B.sc. Hons. Biochemistry

दिल्ली दिश्िदिद्यालय
UNIVERSITY OF DELHI
Bachelor of Science (Hons) Biochemistry
(Effective from Academic Year 2019-20)
Revised Syllabus as approved by
Academic Council
Date: No:
Executive Council
Date: No:
Applicable for students registered with Regular Colleges, Non Collegiate

Women’s Education Board and School of Open Learning
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Syllabus
For
B.Sc. (Honours) Biochemistry
(Three Year Full Time Programme)
Under
Choice Based Credit System (CBCS)

Learning Outcome Based Curriculum Framework
(LOCF)
1st Meeting of Teachers / Faculties (13th Feb 2019)

Course Revision Committee (18th February 2019)
DRAFT 1 (15th March 2019)
DRAFT 2 (22nd April 2019)
1st COC Meeting: 24th April 2019
Draft 3 : (3rd June 2019)
2nd COC Meeting: 4th June 2019
Faculty Meeting : 11th June 2019
Standing Committee : 11th July 2019
(Syllabus applicable for students seeking admission in the B.Sc.

(Hons) Biochemistry Course from the academic year 2019-20)
Department of Biochemistry
Faculty of Interdisciplinary and Applied Sciences
University of Delhi South Campus
New Delhi-110021
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List of Contents Page No.
Preamble 4
1. Introduction to Programme 5
2. Learning Outcome-based Curriculum Framework in Programme

B.Sc. (Hons) Biochemistry
2.1. Nature and Extent of the Programme in B.Sc. (Hons) Biochemistry 6
2.2. Aims of Bachelor Degree Programme in B.Sc. (Hons) Biochemistry 6
3. Graduate Attributes in B.Sc. (Hons) Biochemistry 9
4. Qualification Descriptors for Graduates B.Sc. (Hons) Biochemistry 10
5. Programme Learning Outcomes for in B.Sc. (Hons) Biochemistry 10
6. Structure of in B.Sc. (Hons) Biochemistry 13

6.1. Semester-wise Distribution of Courses 14
6.2. Credit Distribution for B.Sc. (Hons) Biochemistry 15
7. Courses for Programme B.Sc. (Hons) Biochemistry 19-143

7.1. Course Learning Objective
7.2. Course Learning Outcomes
7.3. Course Teaching-Learning Process
7.4. Assessment Methods
8. Keywords 19-143
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PREAMBLE
Biochemistry is the branch of science that explores the chemical processes within and
related to living organisms. It is a laboratory based science programme that brings together
biology and chemistry and focuses on processes happening at the cellular and molecular level.
Biochemistry is the study of the components and composition of living things and their
assembly and interactions important in sustaining life. By using chemical knowledge and
techniques, biochemists attempt to investigate and solve biological problems pertaining to the
understanding of physiological processes, their malfunction leading to diseases and subsequent
disease diagnostics, prevention, therapy and prognostics. Bachelor’s degree in Biochemistry at
University of Delhi endeavors to train students in this classical art of life sciences to create a
knowledge pool and skilled manpower to take on the challenges that modern biological
sciences poses in understanding the emerging dynamics of life processes and the myriads of
diseases that threaten mankind.
Education in the 21st century has undergone a paradigm shift, which necessitates
frequent updates in any curriculum to reflect the dynamic changes in knowledge outcome, more
so for biological sciences where advances are rapid and far-reaching. The revised Choice-
Based Credit System (CBCS) curriculum to be introduced in the academic session 2019-2020
conforms to Learning Outcome Based Curriculum Framework (LOCF) and aims at imparting
concept based learning with emphasis on skill development and research.
For multi-faceted development of a student, the curriculum includes courses to gain

specialization in biochemistry while at the same time obtain sufficient exposure to related and
varied subjects and skills. The curriculum emphasizes on several “core” courses (C) that will
train students with the basic as well as advanced concepts of the discipline of biochemistry. All
students pursuing the Bachelor’s degree with Honours shall study fourteen such core papers
across the six semesters. Students pursuing the programme shall also study four Discipline-
Specific Elective (DSE) courses in the fifth and sixth semesters, which they will select from a
list of such courses based on their individual preferences. These DSE courses will include
diverse papers in other areas of life sciences (like Microbiology and Plant Biochemistry) or
specialized research oriented courses (like Molecular Basis of Infectious Diseases) or advanced
courses of Biochemistry (like Advanced Cell Biology and Advanced Methodologies), which
will provide students with wholesome knowledge and requisite skills preparing them for higher
studies across the globe. The content of each paper (C and DSE papers) is based on the premise
that the fundamental principles and ideas must come across in a clear, easy and concise manner.
The course seeks to be diverse and yet will present the essence of biochemistry in a very elegant
and focused manner that will build competitive edge not only for professional development in
a related area but prepare students for academic pursuits like research and teaching.
The Skill Enhancement Courses (SEC), offered in the third and fourth semesters,
emphasizes on hands-on-training and supplements the discipline courses in an appropriate
manner to impart students the confidence and required skills in practical aspects of
biochemistry to help them choose a future path in either industrial or academic setting. The
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SEC courses also include a paper on research methodology that will prepare students
appropriately for a future in research.
The Generic Elective Courses (GE) offer inter- and trans-disciplinary students an
opportunity to obtain a flavour of Biochemistry in simple and concise terms. It will also help
them to switch over to this discipline of study in the future, should they choose to do so.
Students opting for these courses learn the basic concepts of Biochemistry right from the first
semester onwards, with one paper in each of the first, second, third and fourth semester. .
Students who join for Honours degree in Biochemistry will opt for Generic Elective courses
from other related/unrelated disciplines.
Two value-based courses (Ability Enhancement Compulsory Courses - AECC) in the

first and second semester will enable students to improve their knowledge and communication
skills.
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B.Sc. (Hons) Biochemistry
1. Introduction
Biochemistry is the branch of dynamic science that explores the chemical processes
within living organisms/ systems. The study of Biochemistry aims to understand how all the
molecules that constitute living organisms interact, to maintain and perpetuate life. It deals with
the complexity of living organisms, the microscopic and macroscopic structures within
organisms that have specific functions and their systems for extracting and transforming energy
from the environment. Biochemistry also explains how organisms adapt to their changing
environments and gradually evolve.
The teaching of such a dynamic and evolving course is best achieved through Choice-
based Credit System (CBCS) since it offers opportunities to provide solid foundation in the
core discipline, while allowing freedom to students to select discipline specific courses that
augment the learning in core courses. This freedom is further reiterated through flexibility in
opting courses that enhance specific skills in the discipline as well as selection of courses from
other disciplines / departments that widen the scope for higher education and employability.
The Learning Outcome-based Curriculum Framework (LOCF) built into the CBCS offers
focus and purpose to the programme providing a platform for self-evaluation by students and
teachers in addition to global assessment by all stakeholders. The combination of LOCF and
CBCS also allows for lateral movement of students between institutes of higher learning and
offers a level playing field for them across the nation.
1a. Nature and Extent of the B.Sc. (Honours) Programme in Biochemistry

Biochemistry is an interdisciplinary science with areas of overlap with Chemistry,
Physics and Mathematics. It is a laboratory based science that acts as a bridge between Biology
and Chemistry. It also shares boundaries with other interdisciplinary subjects such as
Microbiology, Genetics and Biophysics. This course is designed so as to enable the students to
gain theoretical knowledge and hands- on-experience in the laboratory. The course content is
aimed at encouraging students to cultivate keen observational skills and to develop the ability
to analyze and interpret experimental data, making them suitable for future careers in higher
education and employment in industry and research institutes.
1b. Aims of the Programme

The overall objective of the Bachelors (Honours) Programme in Biochemistry is to
enable students to learn and integrate foundational knowledge in Biology and Chemistry that
is relevant to Biochemistry and thus prepare them for post-graduate education and /or careers
as researchers in academia or related industries.
The program aims to:
 Provide students with scholarly experiences, both theoretical and hands-on, that help
instil deep interests in learning the chemistry underlying the working of biological
systems while developing broad and balanced knowledge and understanding of key
biological concepts, principles and theories. The idea is to equip students with
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appropriate tools of analysis so that they can independently tackle issues and problems
in the field of biology and chemistry.
 Encourage students to study the structure and function of specific molecules and
pathways and their interactions and networking in biological systems with particular
emphasis on regulation of chemical reactions in living cells.
 Develop in students an inquisitive learning approach to seek answers regarding the
complex workings of various physiological systems, cellular multiplication and
differentiation and communication within and between cells and organs, and the
chemical bases of inheritance and disease.
 Empower students to apply the knowledge and skills they have acquired to the solution
of specific theoretical and applied problems in Biochemistry.
 Build concepts in biochemistry that would enable them to undertake further studies in
Biochemistry and related areas or in multidisciplinary areas and help develop a range
of generic skills that are relevant to wage employment, self-employment and
entrepreneurship.
1c. Program Duration, Design and Structure

Duration of the Program:
The BSc Biochemistry course is a three-year degree programme divided into six
semesters. Each academic year (July - May) will consist of two semesters. Each semester will
be of fifteen weeks duration with one week designated for teaching break to promote co-
curricular and co-scholastic activities.
Program Design:
The program has been designed to offer a variety of discipline specific and
interdisciplinary courses disseminated through class-room, laboratory and out-of-classroom
modes of teaching, monitored through a repertoire of assessment methods. The teaching-
learning process will include theory classes of one hour duration and practical classes of two
hour duration for every credit offered. The curriculum will be delivered through various
methods including classical chalk and talk, power-point presentations, essay writing and quiz
contests, audio and video tools, e-learning and e-content, virtual labs, field trips or educational
tours, seminars by external experts, workshops and symposiums and class discussions and
debates. The learning outcome will be assessed by direct and indirect methods comprising
broadly of Internal Assessment or Continuous Evaluation and End-Semester Examination. The
internal assessment will include mid-term written tests, multiple choice questions, home and
class assignments, oral presentations (seminars), group tasks, class discussions and debates,
essay and report writing. End-semester assessments will include written tests and practical
examinations. Each theory paper will carry a maximum of 100 marks, with 25% marks allotted
for internal assessment and 75% for end-semester examination. Each practical paper will carry
a maximum of 50 marks including experimentation, viva-voce and practical notebook
assessment.
Structure of the Programme:
The programme is structured into a variety of courses with different credits, some
mandatory while others elective. Broadly, the programme comprises of Core Courses (CC) and
elective courses. The core courses are all mandatory courses. The elective courses are of three
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kinds: Discipline-Specific Elective (DSE), Skill Enhancement Course (SEC) and Generic
Elective (GE). The programme also includes two compulsory Ability Enhancement Courses
(AEC).
To successfully complete the program, a student must study fourteen Core Courses,
four Discipline-Specific Electives, two Skill Enhancement Courses, four Generic Elective
Courses and two compulsory Ability Enhancement Courses. The Core Courses, Discipline-
Specific Electives and Generic Electives are six-credit courses. The Skill Enhancement
Courses are four-credit courses while the Ability Enhancement Courses are two credit-courses.
A student has to earn a minimum of 148 credits to get a degree in B.Sc. (H) Biochemistry.
The six-credit courses will include theory classes of four credits each and practicals of
two credits each. The four-credit courses will comprise of two-credit theory classes and two-
credit practical courses. However, the two-credit courses will include only theory classes. One
credit is equivalent to one-hour lecture per week for theory classes and two-hour sessions for
practical classes. Each batch of students for practical sessions will be of fifteen members. If the
number of students exceed fifteen (by at least ten), they will be divided into two equal batches.
It is mandatory for students to study two Core Courses each in Semesters I and II, three
Core Courses each in Semesters III and IV, and two Core Courses each in Semesters V and VI.
The Core Courses will be of six credits each (four credits theory and two credits practicals).
Six courses of Discipline-Specific Electives (DSE) are offered in the programme, of

which students will opt any two in each of the Semesters V and VI. The DSE courses will be
of six credits each (four credits theory and two credits practicals). A particular DSE course will
be offered only if the minimum number of students opting for that course is 10.
Generic Elective (GE) courses for the programme will be offered by other departments
of the respective college. Students will elect one GE course each in Semesters I, II, III, and IV.
The GE courses will be of six credits each (four credits theory and two credits practicals). The
Department of Biochemistry will offer seven GE courses for students of other departments in
the respective colleges.
From a list of six Skill Enhancement (SE) courses provided, students will undertake two
Skill Enhancement (SE) courses of four credits each in Semesters III and IV. The SE courses
will be of four credits each (two credits theory and two credits practicals). The two compulsory
Ability Enhancement Courses (AEC), AE1 (Environmental Sciences) and AE2 (English / MIL
communication), will be of two credits each (theory only). Students will undertake one each in
Semesters I and II.
2. Learning Outcome-based Approach to Curriculum Planning

The learning outcomes-based curriculum framework (LOCF) for a B.Sc. degree in
Biochemistry is intended to provide a broad framework within which the biochemistry
programme is designed such that it enables students to acquire a skill set that helps them
understand and appreciate the field of biochemistry. The structure or design of this framework
shall ensure a high standard of the Honours degree in Biochemistry in the University. It shall
subsequently pave the way for periodic updation and review of the programme, all within the
boundaries of the set framework. This programme specification, as outline in individual
courses, is intended as a reference point for prospective students, current students, examiners
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and academic and support staff involved in delivering the programme and enabling student
development and achievement.
Program learning outcomes are the central organizing features of student learning. They
are developed from the complex interaction of a range of competing and complementary
factors. Since program learning outcomes can only be achieved and demonstrated through
component courses, course learning outcomes and their assessment are integrally related to
program learning outcomes. The expected programme learning outcomes are described below
while the course learning outcomes are included along with course contents. The LOCF in
Biochemistry aims to achieve this important aspect of a modern teaching programme.
3. Characteristic Attributes of a Graduate in Biochemistry

A graduate in the Biochemistry programme is expected to demonstrate the following
attributes:
 Disciplinary knowledge and skills: Capable of demonstrating (i) comprehensive

knowledge and understanding of major concepts, theoretical principles and
experimental findings in Biochemistry and other related fields of study, including
interdisciplinary subfields such as life science in general, medicine and clinical biology,
plant sciences, biotechnology, microbiology, nutrition, forensics, bioinformatics and
environmental science; (ii) ability to use modern instrumentation for chemical and
physical analysis of biological samples.
 Critical thinker and problem solver: Ability to employ critical thinking and efficient
problem solving skills in the various areas of biochemistry and related disciplines.
 Sense of inquiry: Biochemistry being the foundation for understanding all biological
processes, a graduate in this discipline is expected to seek deeper knowledge by asking
relevant/appropriate questions relating to issues and problems in the field of
Biochemistry and related areas. It is also envisaged that the course will empower them
with the ability to plan, execute and report the results of an experiment or investigation.
 Research skills: Capable of identifying a scientific problem, preparing/mobilising
appropriate resources required for the project, and execute the project through to
completion, while observing responsible and ethical scientific conduct; and biosafety
and chemical hygiene regulations and practices.
 Skilled communicator: Ability to transmit complex technical information relating to
biochemistry in a clear and concise manner in both oral and written formats.
 Team player/worker: Capable of working effectively in diverse teams in both
classroom, laboratory and in industry and field-based situations.
 Digitally literate: Capable of using computers for mining scientific information using
modern library search tools from various open source platforms or journals and the
ability to use technique specific software to conduct experiments and analyze data. The
graduates are expected to be proficient in using computational & visualization tools to
study bio-molecular structures, graphing and statistical software to analyze statistical
significance of data and report data in the form of graphs, tables or figures.
 Ethical awareness: The graduates of this programme will be able to avoid unethical
behaviour such as fabrication, falsification or misrepresentation of data or committing
plagiarism. They will learn to appreciate environmental and sustainability issues and
their societal relevance.
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 Lifelong learners: Capable of self-paced and self-directed learning aimed at personal
development and for improving knowledge/skill development and acquiring fresh
skills.
4. Qualification Description
The qualification descriptors for B.Sc. (Honours) programme in Biochemistry include
the following:
 A student should demonstrate (i) a comprehensive and coherent understanding of the

field of Biochemistry, its applications and links to related disciplinary areas of study;
(ii) practical knowledge that enables different types of professions related to the
discipline, including research and development, teaching, entrepreneurship as well as
industrial research abilities; (iii) skills in areas pertaining to current developments in
the academic field of study, including a critical understanding of the latest
developments in the field of Biochemistry and an ability to use established techniques
of analysis.
 Demonstration of a comprehensive knowledge of study material, including current
research articles, books and e-books relating to basic and advanced concepts.
 Demonstration of skills in collection of relevant data gathered by reading or
experimentation and analysis and interpretation of the data using appropriate
methodologies.
 Ability to communicate the results of studies undertaken in an academic field
accurately in the form of a paper, oral presentation or report.
 Application of disciplinary knowledge and transferable skills to new or unfamiliar
problems and issues and the ability to seek solutions to real-life problems.
 Imbibing the ability to function effectively either independently or as a constituent
of a team.
5. Programme Learning Outcomes (PO)

The curriculum is designed to achieve the following outcomes:
PO1: Inculcate the basic concepts of biochemistry including an understanding of the

fundamental biochemical principles and their applications in a systematic, methodical,
scientific, evidence-based process. The programme will also provide a general understanding
of the related disciplines with a holistic knowledge generation in biological sciences.
PO2: Develop problem solving and analytical skills through case studies, research papers and
hands-on-experience, especially integrated into skill enhancement courses.
PO3: Students will gain proficiency in basic laboratory techniques and be able to apply the
scientific method to the processes of experimentation, hypothesis testing, data interpretation
and logical conclusions.
PO4: Provide requisite knowledge of laboratory safety, data replication and quality control,
record keeping and other aspects of “responsible conduct of research”.
PO5: Ability to employ modern library search tools to locate and retrieve primary literature on
a topic and critically evaluate the literature.
PO6: Students will be able to apply and effectively communicate scientific reasoning and data
analysis in both written and oral forms. They will be able to communicate effectively with
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well-designed posters and slides in talks aimed at scientific audiences as well as the general
public.
PO7: Students will learn to work collaboratively in a team.
PO8: Students will gain knowledge of ethical and good laboratory practices, health and
biohazard regulations, plagiarism and intellectual property rights related issues practiced in
modern era of scientific investigation.
PO9: Graduates will be able to apply the major theories and research procedures to
contemporary societal issues.
P10: The programme will prepare students to plunge into various fields of higher education or
related profession in various disciplines, armed with plethora of knowledge, hands-on-
experience and scientific attitude, at national and global levels.
6. Teaching-learning processes
The foremost effort of teaching is to impart knowledge to students, factual as well as
hypothetical. The manner in which this is communicated to the students determines the success
of the teaching process. To be able to see tangible results, it is imperative that the teaching-
learning process be bilateral. There are three critical components to the teaching learning
process, namely content writing, content delivery and engaging the students to complete the
course. A passive flow of information from the teacher to the taught should make way for a
vibrant atmosphere of active participation from the students. Teachers participating in the
programme would have a well-structured and well-planned lecture ready for the class that
should compel the students to concentrate, understand and enjoy the discourse. Students would
be encouraged to think independently and ask pertinent questions cultivating out-of-the-box
thinking. The link between theory and practical would be made evident, as working with their
hands reinforces the concepts first introduced in theory classes.
The traditional chalk and talk method of teaching is simple but very effective. Diagrams
or additional material may be shown as slides but with minimum text-rich content. For concepts
that are difficult to explain, power point presentations or videos would be used. Some
laboratory experiments will be open ended. Students will be divided into small groups to
encourage teamwork, healthy competition and to be able to complete the task in stipulated time
frames. Students will be taken out of the classroom and into the world of research institutions
as well as industries in the form of simple visits or internships or educational tours for
maximum benefit. It will help them to correlate what they learn in the classroom with the real
world. Additionally, teachers will use MOODLE platform to create lessons and interact with
students to create an open and effective two-way communication channel. Digital initiatives
such as the Swayam portal, National digital library and open education resources will be used
to greatly facilitate blended learning and flipped class rooms encouraging students to be
responsible for learning. Group discussions, debates and scientific talks by external experts
will be arranged for facile learning. Students will be encouraged to write comprehensive
reviews of papers in a particular topic, reports, essays and short projects to augment their
writing skills. Students will also be motivated to deliver seminars to strengthen their oratory
skills.
7. Assessment methods
Assessment methods are the strategies, techniques, tools and instruments for collecting
information to determine the extent to which students demonstrate desired learning outcomes.
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Student learning outcomes cannot be ascertained by single evaluation criteria. A combination
of direct and indirect assessments would thus be used. Direct methods of assessment will be
used for students to demonstrate their learning while indirect methods will be used to observe
students reflect on their learning. Written tests, essays, quiz, presentations and seminars will
be used as direct methods of assessment, and indirect methods will include surveys,
discussions, debates, participation in scientific meetings and festivals. Embedded assessments,
in other words “classroom-based” or “continuous” assessments will be utilized as both a
grading instrument as well as data for assessing student learning outcomes. Some examples of
assessment methods that will be used are given below:
Method Description Direct or

Indirect
Assessment
Attendance Regular participation in class activities (Theory and Indirect
Practicals)
Observations Information can be collected while observing Indirect
“events” such as classes, group work, and study
sessions.
Performance Students can be evaluated on participation in Direct
practicals, events, presentations, projects. Encourages
public speaking skills.
Portfolio Students’ work is collected throughout the program Direct
which is assessed by faculty using a common scoring
guide. Portfolios may contain assignments, reports,
class tests, exams, case studies, presentations,
practical file record etc.
Viva Voce or An interview conducted by external faculty to gauge Indirect
External Review the depth of theoretical knowledge, clarity,
visualization and hands on practical skills of the
student. Instills self-confidence to face interviews in
their future careers.
Internally These are shorter tests held periodically through the Direct
developed class semester to assess how well the students have grasped
tests the concepts and skills. Also encourages regular
attendance.
Course Exam A comprehensive written exam given near the end of Direct
every 2 semesters to determine a student’s acquisition
and application of a particular type of knowledge or
skill, as well as the ability to integrate knowledge.
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Structure of B.Sc. (Honours) Biochemistry under CBCS
Core Course
BCH C-1: Molecules of Life
BCH C-2: Cell Biology
BCH C-3: Proteins
BCH C-4: Enzymes
BCH C-5: Metabolism of Carbohydrates and Lipids
BCH C-6: Membrane Biology and Bioenergetics
BCH C-7: Hormone: Biochemistry and Function
BCH C-8: Human Physiology
BCH C-9: Gene Organization, Replication and Repair
BCH C-10: Metabolism of Amino Acids and Nucleotides
BCH C-11: Concepts in Genetics
BCH C-12: Gene Expression and Regulation
BCH C-13: Genetic Engineering and Biotechnology
BCH C-14: Immunology
Discipline Specific Elective (Any four)
BCH DSE-1: Nutritional Biochemistry

BCH DSE-2: Advanced Cell Biology
BCH DSE-3: Microbiology
BCH DSE-4: Molecular Basis of Infectious Diseases
BCH DSE-5: Plant Biochemistry
BCH DSE-6: Advanced Methodologies
Generic Elective (Any four)
BCH GE-1: Biomolecules

BCH GE-2: Techniques in Biochemistry
BCH GE-3: Proteins and Enzymes
BCH GE-4: Biochemical Correlation of Diseases
BCH GE-5: Intermediary Metabolism
BCH GE-6: Biochemical Applications in Forensics
BCH GE-7: Recombinant DNA Technology
Ability Enhancement Compulsory Course

AECC-1: English / MIL communication
AECC-2: Environmental science
Skill Enhancement Elective Course (Any two)
BCH SEC-1: Biochemical Techniques

BCH SEC-2: Biostatistics
BCH SEC-3: Research Methodology
BCH SEC-4: Bioinformatics
BCH SEC-5: Microbial Techniques
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SEMESTER-WISE COURSE STRUCTURE of B.Sc. (Honours) Biochemistry
SEMESTER I SEMESTER II
C1 Molecules of Life C3 Proteins
C2 Cell Biology C4 Enzymes
AECC1 English/MIL Communication or EVS AECC2 English/MIL Communication or EVS
GE-I Generic Elective (Any one) GE-II Generic Elective (Any one)
I. Biomolecules (GE-1) I. Proteins and Enzymes (GE-3)
II. Techniques in Biochemistry (GE- II. Techniques in Biochemistry (GE-
2) 2A)
III. Biochemical Correlation of
Diseases (GE-4)
SEMESTER III SEMESTER IV
C5 Metabolism of Carbohydrates and C8 Human Physiology
Lipids
C6 Membrane Biology and Bioenergetics C9 Gene Organization, Replication and
Repair
C7 Hormone: Biochemistry and Function C10 Metabolism of Amino Acids and
Nucleotides
SEC-I Skill Enhancement Course (Any one) SEC-II Skill Enhancement Course (Any one)
I. Biochemical Techniques (SEC-1) I. Bioinformatics (SEC-4)
II. Biostatistics (SEC-2) II. Microbial Techniques (SEC-5)
III. Research Methodology (SEC-3) III. Research Methodology (SEC-3A)
GE-III Generic Elective (Any one) GE-IV Generic Elective (Any one)
I. Intermediary Metabolism (GE-5) I. Biochemical Correlation of
Diseases (GE-4A)
II. Proteins and Enzymes (GE-3A) II. Recombinant DNA Technology
(GE-7)
III. Biochemical Applications in III. Biochemical Applications in
Forensics (GE-6) Forensics (GE-6A)
SEMESTER V SEMESTER VI
C11 Concepts in Genetics C13 Genetic Engineering and
Biotechnology
C12 Gene Expression and Regulation C14 Immunology
DSE-I Discipline Specific Elective (Any two) DSE-II Discipline Specific Elective (Any two)
I. Nutritional Biochemistry (DSE-1) I. Molecular Basis of Infectious
Diseases (DSE-4)
II. Advanced Cell Biology (DSE-2) II. Plant Biochemistry (DSE-5)
III. Microbiology (DSE-3) III. Advanced Methodologies (DSE-
6)
C: Core Courses (14); GE: Generic Elective (04); AECC: Ability Enhancement Compulsory Course (02);
SEC: Skill Enhancement Courses (02); DSE: Discipline Specific Elective (04). Numbers within
bracket indicate the total number of courses offered in each category.
Courses containing “A” in their course code are repeated in different semesters.
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SCHEME FOR CHOICE BASED CREDIT SYSTEM IN
B.Sc. HONOURS BIOCHEMISTRY
SEMESTER COURSES OFFERED COURSE NAME CREDITS

I Ability Enhancement Compulsory English / MIL 4
Course 1 communication /
Environmental
Science
Core course 1 Theory (C1) Molecules of Life 4
Core course 1 Practical Molecules of Life 2
Core course 2 Theory (C2) Cell Biology 4
Core course 2 Practical Cell Biology 2
Generic Elective 1 Theory (GE-1) Biomolecules 4
Generic Elective 1 Practical Biomolecules 2
Generic Elective 2 Theory (GE-2) Techniques in 4
Biochemistry
Generic Elective 2 Practical Technique in 2
Biochemistry
II Ability Enhancement Compulsory English / MIL 4
Course 2 communication /
Environmental
Science
Core course 3 Theory (C3) Proteins 4
Core course 3 Practical Proteins 2
Core course 4 Theory (C4) Enzymes 4
Core course 4 Practical Enzymes 2
Generic Elective 3 Theory (GE-3) Proteins and 4
Enzymes
Generic Elective 3 Practical Proteins and 2
Enzymes
Generic Elective 4 Theory (GE-4) Biochemical 4
Correlation of
Diseases
Generic Elective 4 Practical Biochemical 2
Correlation of
Diseases
III Core course 5 Theory (C5) Metabolism of 4
Carbohydrates and
Lipids
Core course 5 Practical Metabolism of 2
Carbohydrates and
Lipids
Core course 6 Theory (C6) Membrane Biology 4
and Bioenergetics
Core course 6 Practical Membrane Biology 2
and Bioenergetics
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Core course 7 Theory (C7) Hormone: 4
Biochemistry and
Function
Core course 7 Practical Hormone: 2
Biochemistry and
Function
Skill Enhancement Course -1 Biochemical 2
Theory (SEC-1) Techniques
Skill Enhancement Course -1 Biochemical 2
Practical Techniques
Skill Enhancement Course -2 Biostatistics 2
Theory (SEC-2)
Skill Enhancement Course -2 Biostatistics 2
Practical
Skill Enhancement Course -3 Research 2
Theory (SEC-3) Methodology
Skill Enhancement Course -3 Research 2
Practical Methodology
Generic Elective – 5 Theory (GE-5) Intermediary 4
Metabolism
Generic Elective – 5 Practical Intermediary 2
Metabolism
Generic Elective – 6 Theory (GE-6) Biochemical 4
Applications in
Forensics
Generic Elective – 6 Practical Biochemical 2
Applications in
Forensics
IV Core course 8 Theory (C8) Human Physiology 4
Core course 8 Practical Human Physiology 2
Core course 9 Theory (C9) Gene organization, 4
replication and repair
Core course 9 Practical Gene organization, 2
replication and repair
Core course 10 Theory (C10) Metabolism of 4
Amino Acids and
Nucleotides
Core course 10 Practical Metabolism of 2
Amino Acids and
Nucleotides
Skill Enhancement Course – 4 Bioinformatics 2
Theory (SEC-4)
Skill Enhancement Course – 4 Bioinformatics 2
Practical
Skill Enhancement Course – 5 Microbial Techniques 2
Theory (SEC-5)
Skill Enhancement Course – 5 Microbial Techniques 2
Practical
16
Generic Elective – 7 Theory (GE-7) Recombinant DNA 4
Technology
Generic Elective - 7 Practical Recombinant DNA 2
Technology
V Core course 11 Theory (C11) Concepts in Genetics 4
Core course 11 Practical Concepts in Genetics 2
Core course 12 Theory (C12) Gene expression and 4
regulation
Core course 12 Practical Gene expression and 2
regulation
Discipline Specific Elective-1 Nutritional 4
Theory (DSE-1) Biochemistry
Discipline Specific Elective-1 Nutritional 2
Practical Biochemistry
Discipline Specific Elective-2 Advanced Cell 4
Theory (DSE-2) Biology
Discipline Specific Elective – 2 Advanced Cell 2
Practical Biology
Discipline Specific Elective – 3 Microbiology 4
Theory (DSE-3)
Discipline Specific Elective – 3 Microbiology 2
Practical
VI Core course 13 Theory (C13) Genetic Engineering 4
and Biotechnology
Core course 13 Practical Genetic Engineering 2
and Biotechnology
Core course 14 Theory (C14) Immunology 4
Core course 14 Practical Immunology 2
Discipline Specific Elective-4 Molecular basis of 4
Theory (DSE-4) infectious diseases
Discipline Specific Elective-4 Molecular basis of 2
Practical infectious diseases
Discipline Specific Elective-5 Plant Biochemistry 4
Theory (DSE-5)
Discipline Specific Elective-5 Plant Biochemistry 2
Practical
Discipline Specific Elective – 6 Advanced 4
Theory (DSE-6) Methodologies
Discipline Specific Elective – 6 Advanced 2
Practical Methodologies
Total : 148 credits
Note: 1 Credit is equivalent to 1 hour of teaching per week for theory courses and 2 hour of
teaching for practical courses.
17
B.Sc. (HONOURS) BIOCHEMISTRY (CBCS STRUCTURE)
CORE COURSES
18
CORE PAPER
Molecules of Life (BCH C-1)
Semester - I
1. Course Objectives
The course aims to provide students with an understanding of biomolecules, the basic
building blocks of living organisms, focusing on their structural underpinnings, unique
properties, biological roles and functions and inter relations. The course will outline the
importance of water as a biological solvent and vitamins as vital ingredients of life. Emphasis
will be on the association between structure and function of various biomolecules at a chemical
level with a biological perspective as well as hands on approach and laboratory techniques.
2.1 Course Learning Outcomes
On successful completion of the course students will be:
 Acquainted with chemical and molecular foundations of life and appreciate the role of
water in biological systems.
 Able to comprehend the structure, function and acid base properties of amino acids.
 Introduced to the structure, properties and roles of carbohydrates, lipids and nucleic
acids.
 Aware of the importance of vitamins in biological systems.
 Able to independently identify various biomolecules in the laboratory.
2.2 Course Contents
THEORY
CREDITS: 4 TOTAL HOURS: 60
UNIT I : The foundations of biochemistry No. of hours : 6
Cellular and chemical foundations of life, Water: unique properties, weak interactions in
aqueous systems, ionization of water, buffering action in biological system, water as a reactant
and fitness of the aqueous environment.
UNIT II: Amino Acids No. of hours : 8
Structural features and classification; Physical properties, optical properties

(Stereoisomerism); Chemical properties (acid base properties, titration curve) of amino acids;
Uncommon amino acids and their functions
UNIT III: Carbohydrates and Glycobiology No. of hours : 16
Monosaccharides - structure of aldoses and ketoses; Ring structure of sugars, conformations of

sugars, mutarotation, anomers, epimers and enantiomers; Structure of biologically important
19
sugar derivatives, oxidation and reduction of sugars; Formation of disaccharides, reducing and
non-reducing disaccharides; Polysaccharides – homo- and heteropolysaccharides, structural
and storage polysaccharides; Structure and role of glycoconjugates - proteoglycans,
glycoproteins and glycolipids (gangliosides and lipopolysaccharides); Carbohydrates as
informational molecules.
UNIT IV: Lipids No. of hours : 14
Building blocks of lipids - fatty acids, glycerol, ceramide; Storage lipids - triacyl glycerol and
waxes; Structural lipids in membranes – glycerophospholipids; Galactolipids and sulpholipids,
etherlipids, sphingolipids and sterols, structure, distribution and role of membrane lipids. Plant
steroids; Lipids as signals, cofactors and pigments. Qualitative tests for lipids.
UNIT V: Nucleic Acids No. of hours : 10
Nucleotides - structure and properties of bases, pentoses, nucleosides; Nucleic acid structure –
Watson-Crick model of DNA, forms of DNA; Structure of major species of RNA - mRNA,
tRNA and rRNA; Nucleic acid chemistry - UV absorption, effect of acid and alkali on DNA;
Other functions of nucleotides - source of energy, component of coenzymes and second
messengers.
Unit VI: Vitamins No. of hours : 6
Structure and active forms of water soluble and fat soluble vitamins; Deficiency diseases and
symptoms, hypervitaminosis
PRACTICALS
1. Safety measures in laboratories.

2. Preparation of normal and molar solutions.
3. Preparation of buffers, phosphate and acetate buffers.
4. Determination of pKa of acetic acid and glycine.
5. Qualitative tests for carbohydrates.
6. Qualitative tests for amino acids, proteins.
7. Qualitative tests for nucleic acids.
8. Separation of amino acids/ sugars/ bases by thin layer chromatography/paper
chromatography.
9. Estimation of vitamin C.
2.3 References
1. Devlin, T.M. (2011). Textbook of Biochemistry with Clinical Correlations (7th ed.).
New York, John Wiley & Sons, Inc. ISBN:978-0-470-28173-4.
2. Nelson, D.L., Cox, M.M. (2017). Lehninger: Principles of Biochemistry (7th ed.). New
York, WH: Freeman and Company. ISBN: 13: 978-1-4641-2611-6 / ISBN:10:1-
46412611-9.
20
3. Teaching Learning Process and Assessment Methods
Facilitating the Achievement of Course Learning Outcomes**
Unit Course Learning Teaching and Learning Assessment Tasks

No. Outcomes Activity
I. Appreciation of the Traditional chalk and board Unit assessment by
role of water in teaching and hands-on- multiple choice questions
biological system. experiments with buffers (MCQ)
II. Ability to Classroom teaching of Quiz on amino acid
comprehend the structures and properties of properties and structure.
structure, function amino acids and laboratory Students will be shown
and acid base experiments on titration curvesthree-dimensional
properties of amino and identification of functional
structures of amino acids
acids. groups in power points, which
they will identify and
relate to properties
III. Introduction to the Traditional chalk and board Test on structure and
structure, properties teaching; learning properties of functions of carbohydrates
and roles of carbohydrates through
carbohydrates. laboratory based identification
IV Appreciation of the Traditional teaching of Test and MCQ on lipids
varied roles of lipids structures of lipids and video
including presentation of membrane
distribution in lipids: learning structure and
different biological function of lipids and
membranes membranes through discussion
and power point presentations
V. Understanding Chalk and board teaching and Test and quiz on nucleic
nucleic acid presentation on double helix acids. Discussion on the
chemistry and model of nucleic acid history of discovery of
structure. structure. double helix of DNA
VI. Understanding of the Classroom teaching of vitamin Quiz on vitamins, their
biochemical structures and their active active forms and
importance of forms and estimation of deficiency diseases.
vitamins and their vitamin-C in laboratory Revision of the entire
active forms course
(**Assessment tasks enlisted here are indicative in nature)
4. Keywords
Carbohydrates; Lipids; Nucleic acids; Amino acids; Vitamins; Water; Buffers
21
CORE PAPER
Cell Biology (BCH C-2)
Semester I
The objective of this paper is to offer insights into the basic structure and function of a
cell and cellular organelles. The course also aims to impart understanding of cell cycle, cell
death, cell renewal processes and various techniques of cell biology.
The objective of this paper is to offer insights into the basic structure and function of a
cell and cellular organelles. Students will:
 Learn about cell theory and basic cell structure

 Be introduced to cell fractionation and cell visualization techniques
 Gain knowledge about the structure and function of various cell organelles in a
eukaryotic cell
 Acquire knowledge about the composition of cytoskeleton and extracellular matrix
 Acquire insight into cell division and cell death mechanisms
THEORY
UNIT I: Introduction to Cell Biology No. of hours: 5
Cell theory, Structure of prokaryotic and eukaryotic cell, exceptions to cell theory,
mycoplasma, viruses, viroids, prions, cells as experimental models
UNIT II: Tools of Cell Biology No. of hours: 10
Cell Fractionation techniques: Principle of centrifugation, Sedimentation Coefficient,

Differential and Density Gradient (isopycnic and rate zonal) centrifugation. Cell Visualization
techniques: Principle of Light microscope, Phase Contrast microscope, Fluorescence
microscope, Confocal microscope and Electron microscope; Sample preparation and staining
techniques for different kinds of microscopy. Basic principles of identification of sub cellular
organelles.
UNIT III: Cell Organelles (structure and function) No. of hours: 17
Nucleus: Structure of nuclear envelope, nuclear pore complex nucleolus and chromatin
Endoplasmic Reticulum: RER - Brief overview of cotranslational and post-translational
transport of proteins; SER – Lipid synthesis, brief overview of export of proteins from ER;
Golgi apparatus: organization, brief overview of glycosylation of proteins within Golgi, lipid
and polysaccharide metabolism in Golgi apparatus.
22
Lysosomes: Development of different forms of lysosomes, role in cellular digestion, lysosomal
storage diseases Peroxisomes: assembly, functions (H2O2 metabolism, fatty acid oxidation),
glyoxysomes Mitochondria: structure, endosymbiont theory, genome Chloroplast: structure,
endosymbiont theory, genome
UNIT IV: Cell Wall, Extracellular Matrix and Cell Junctions No. of hours: 10
Prokaryotic and eukaryotic cell wall structure; ECM components – proteins, polysaccharides
and adhesion molecules; basic concept of anchoring junctions, tight junctions and
communication junctions (gap junctions and plasmodesmata)
UNIT V: Cytoskeleton No. of hours: 08
Structure, assembly and function of Microtubules: Axonemal and cytoplasmic microtubules

(cilia, flagella, centrioles, basal bodies) Microfilaments: Actin and Myosin Intermediate
Filaments: different classes. Role of cytoskeletal elements in the entry of infectious agents
UNIT VI: Cell Cycle, Cell Death and Cell Renewal No. of hours: 10
Eukaryotic Cell Cycle, Checkpoints, Cell Division (mitosis and meiosis); Brief overview of
apoptosis and necrosis; Types and potency of Stem Cells, Cancer – types, salient features of a
transformed cell, causes of cancer. Apoptotic death in relation to cell cycle
PRACTICALS
CREDIT : 2 TOTAL HOURS: 60
1. To study the parts of a microscope

2. Cytochemical staining of proteins by Methylene Blue
3. Cytochemical staining of RNA by Methyl Green Pyronin
4. Cytochemical staining of polysaccharides by PAS
5. To study different stages of mitosis by temporary preparation in onion root tip
6. To study different stages of meiosis by temporary preparation in onion flower buds/
grasshopper testes
7. To study cell organelles by using electron micrographs
8. To study the effect of isotonic, hypotonic and hypertonic solution on cells
2. References
1. Cooper, G.M., Hausman, R.E. (2013). The Cell: A Molecular Approach (6th ed.).
Washington, DC: ASM Press & Sunderland, Sinauer Associates, MA. ISBN:978-0-
87893-300-6.
Additional Resources:
1. Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., Walter, P. (2008) Molecular
Biology of the Cell (5th ed.). New York: Garland Science (Princeton). ISBN:0-8153-
1619-4 / ISBN:0-8153-1620-8.
2. Karp, G. (2013). Cell and Molecular Biology: Concepts and Experiments (7th ed.). John
Wiley and Sons. Inc. ISBN: 978-1-118-65322-7
23

I. Students will learn Milestones of the development Students will be asked to
about the cell theory in cell biology will be research on this topic.
and basics of cell discussed, Models of cell Assignments will be
structure structure will be shown conducted
II. Students will be Students will be taught by use Quiz will be organized.
introduced to cell of video tutorial. They will beThey will be shown
fractionation and cell taken to various institutes forvarious pictures to identify
visualization demonstration of some of the the various microscopy
techniques tools taught in class techniques. Assignment
and tests.
III. Students will gain Will be taught by chalk and They will be asked to label
knowledge about the board method. Students will be various parts of organelles.
structure and shown various power point Assignment and tests will
function of various presentations and videos for be conducted.
cell organelles in a concept building
eukaryotic cell
IV. Students will gain Teaching will be imparted by Students will be assigned
knowledge about the chalk and board method and the task of retrieving
structure of cell wall, by videos. information on the
components of differences in cell wall in
extracellular matrix various kingdom of life
and basics of cell and enlist the components
junctions of extracellular matrix.
V. Students will acquire Chalk and board method of Students will be assigned
knowledge about the teaching to be employed along the task of retrieving
structure, with power point presentations information on
composition and and videos. cytoskeleton elements and
significance of their relation to diseases
cytoskeleton
VI. Students will acquire Power point presentations, Assignment and tests;
insight into cell video tutorials and traditional identification of different
division and cell teaching will be utilized. stages of cell division and
death mechanisms Current research in this area cell death will be assigned
will be discussed in groups
4. Keywords
Cell organelles, Cell wall, Cell-Cell Interactions, Cancerous Cells, Cell-Pathogen

interactions, Cell Theory, Cell cycle, Transformed cell
24
CORE PAPER
Proteins (BCH C-3)
SEMESTER –II
The course aims to introduce “proteins” and their importance to modern biochemistry,
highlighting their structural features and unique characteristics that help them participate in
every physiological process in life, thus also playing important role in disease manifestation
and their interventions.
After completion of the course, a student will
 Understand the diverse functions of proteins in a cell

 Understand the hierarchy of protein architecture – primary, secondary, tertiary &
quaternary structure, with the ability to distinguish features of globular & fibrous
proteins
 Be able to comprehend the fundamental mechanisms of protein folding and stability
and their relation to conformational diseases
 Be able to describe and discuss the separation and purification techniques used in
protein chemistry
 Learn to access and use the databases related to protein sequence and structure
 Understand specialized proteins like membrane proteins, defense proteins and motor
proteins
 Gain comprehension of structure-function relationship of proteins and their
significance in physiology, diseases and applications in industry and medicine.
2.2 Course Contents
THEORY
UNIT I: Introduction to amino acids, peptides and proteins No. of hours: 4
Amino acids and their properties - hydrophobic, polar and charged. Multimeric proteins,
Conjugated proteins and Metallo-proteins. Diversity of peptide and protein function and their
applications. Solid phase peptide synthesis.
UNIT II: Hierarchy of protein structure No. of hours: 18
Organization of protein structure into primary, secondary, tertiary and quaternary structures.
N-terminal and C-terminal amino acid analysis. Sequencing techniques - Edman degradation.
Generation of overlap peptides using different enzymes and chemical reagents. Disulfide bonds
and their location. Forces stabilizing the protein structure - covalent and non-covalent.
Importance of primary structure in protein folding. The peptide bond, dihedral angles psi and
25
phi, helices, sheets and turns, Ramachandran map. Motifs and domains. Structures of
myoglobin and haemoglobin, α-keratin, silk fibroin, collagen.
UNIT III: Protein folding and conformational diseases No. of hours: 6
Denaturation and renaturation of Ribonuclease A – discovery of protein folding. Introduction

to thermodynamics of folding and molten globule. Assisted folding by molecular chaperones,
chaperonins and PDI. Defects in protein folding. Diseases associated with misfolding –
Alzheimer’s and Prion based.
UNIT IV: Specialized proteins No. of hours: 10
Transport protein: Haemoglobin - Oxygen binding curves, influence of 2,3-BPG, CO2 and H+,
Hill plot, Cooperativity between subunits and models to explain the phenomena - concerted
and sequential models. Haemoglobin disorders-sickle cell anemia, thalassemias. Motor
proteins- Actin and myosin. Defense proteins- Antibodies, Membrane proteins- Integral and
membrane associated proteins. Hydropathy plots to predict transmembrane domains.
UNIT V: Extraction, purification and characterization of proteins No. of hours: 18
Solubilization of proteins from their cellular and extracellular locations. Use of mechanical and
chemical methods, homogenization, ultrasonication, French press and centrifugation.
Ammonium sulphate fractionation, solvent fractionation, dialysis and lyophilization Ion-
exchange chromatography, molecular sieve chromatography, hydrophobic interaction/reverse
phase chromatography, affinity chromatography, HPLC and FPLC. Determination of purity,
molecular weight, extinction coefficient and sedimentation coefficient. IEF, SDS-PAGE and
2-D gel electrophoresis.
UNIT VI: Introduction to Protein Databases No. of hours: 4
Introduction to protein sequence and structure databases (UNIPROT, SWISS-PROT & PDB),
Protein sequence file Format (FASTA) and Visualization softwares.
PRACTICALS
1. Estimation of proteins using UV-absorbance and Biuret method.

2. Estimation of proteins using Lowry/Bradford method.
3. Determination of isoelectric pH of casein.
4. Ammonium sulphate fractionation of proteins.
5. Separation of proteins using anion-exchange chromatography (demonstration).
6. SDS-PAGE analysis of proteins (demonstration).
7. Molecular Visualization Softwares: Pymol and Rasmol for protein structures from PDB
2.3 References
1. Cooper, T.G. (2011). The Tools of Biochemistry. Wiley India Pvt. Ltd
York, WH: Freeman and Company. ISBN13: 9781464126116, ISBN10: 1464126119
26
3. Schulz, G.E., Schirmer, R.H. (1979). Principles of protein structure. Springer, ISBN
978-1-4612-6137-7
4. Scopes, R.K. (1994) Protein Purification. Principles and Practice (3rd ed). Springer,
ISBN 978-1-4737-2333-5
5. Stryer, L., Berg, J., Tymoczko, J., Gatto, G. (2019). Biochemistry (9th ed.). New York,
WH: Freeman. ISBN-13: 9781319114671
6. Voet, D., Voet. J. G. (2013). Biochemistry (4th ed.). New Jersey, John Wiley & Sons
Asia Pvt. Ltd. ISBN : 978-1-11809244-6.
Additional Resources
1. Whitford, D. (2004). Protein Structure and function. Southern Gate, Chichester, West
Sussex: John Wiley & Sons, Inc. ISBN-13: 978-047149894 ISBN-10: 0471498947

I. Appreciation of the Outlining history of Numerical problems
significance of proteins development of proteins related to codes in amino
in life; Understanding through power point acids, numerical problems
of the classification presentations and landmark relating to the pKa and pI
and diversity of publications; Classification of amino acids.
functions of proteins; and diversity will be taught
Knowledge of amino by chalk and board method;
acids as building Stereochemistry models for
blocks of proteins, amino acids structures and
their classification and power point presentations
structures and videos
II. Knowledge of Traditional chalk and board Numerical problems on
hierarchy of protein method will be employed Sequencing will be
structures and various along with powerpoint assigned; Students will
aspects of structures presentations on 3D download 3D structures
and sequencing structures, Ramachandran from PDB and visualize
methods; concepts of Map and hierarchy of protein several aspects of
subunits with reference structures; Videos will be structures using softwares.
to hemoglobin shown
structure
III. Basic concepts as to Appropriate mix of chalk Class presentations and
how proteins fold and and board teaching as well as case studies will help
what challenges they use of Power point students understand
face during folding; presentations for clarity of misfolding diseases; They
Knowledge about concepts with images; will be asked to match a
chaperones that help in Research papers will be few proteins with the
protein folding and discussed diseases they cause due to
diseases caused due to misfolding. Each student
protein misfolding will review a paper on the
biotechnological
27
importance of refolding of
proteins in vitro
IV Students will learn Power point presentations; Images of proteins to
about the structural Chalk and board; Student identify globular and
features and interaction in class; Case fibrous proteins will be
differences between studies with examples of provided. Transmembrane
fibrous and globular each protein structural class protein prediction tools
proteins with will be used by students,
examples; Structural Hydropathy plots will be
aspects of membrane discussed.
proteins and their
relation to function
V. Development of Chalk & board method of Numerical methods to
understanding of the teaching followed by class discuss enzyme activity,
rationale, basic discussions with examples. specific activity will
principles, types of assigned; Practical
biochemical and problems in protein
biophysical methods purification will be
for extraction and discussed and assigned in
characterization of groups
proteins
VI. Students will learn Power point presentations on Assignments and quiz on
about protein databases various databases, protein databases and tools used in
and tools available in sequence and structure protein sequence and
public domain. retrieval to be utilized. structure analysis;
Students will be assigned
the task of identifying new
databases and tools by
browsing papers and
internet.
4. Keywords
Amino acids, Peptides; Globular and Fibrous proteins; Protein structure; Denaturation
and Renaturation; Purification of proteins; Protein Folding & Diseases; Protein Databases
28
CORE PAPER
Enzymes (BCH C-4)
Semester - II
The objective of the course is to provide detailed knowledge about enzymes, the
biological catalysts with remarkable properties that sustain life, so as to develop an
understanding of enzyme kinetics, mechanism of enzyme action and their regulation. The
course also aims to outline the diverse applications of enzymes in disease diagnosis and therapy
as well as in industry.
 Students will learn the nature and importance of enzymes in living systems
 Students will gain insight into the thermodynamic and molecular basis of catalysis by
enzymes and the underlying basis of their specificity
 Students will understand the mechanisms of enzyme action, kinetics of enzyme
catalyzed reactions and clinical importance of enzyme inhibitors
 Students will also learn to appreciate how enzymes are regulated and the physiological
importance of enzyme regulation in the cell
 The course will introduce students to the applications of enzymes in research and
medicine as well as in industry, which will bolster their foray into industrial and
biomedical research.
2.2 Course Contents
THEORY
UNIT I: Introduction to enzymes and features of catalysis No. of hours: 8
General characteristics of enzymes; nature of enzymes - protein and non-protein (ribozymes –

RNaseP, self-splicing introns, abzymes). Co-factor and prosthetic group, apoenzyme,
holoenzyme. Classification and nomenclature of enzymes. Enzyme assays-discontinuous,
continuous, coupled assays; Enzyme activity, specific activity, units to express enzyme
activity. Features of enzyme catalysis, factors affecting the rate of chemical reactions, collision
theory, activation energy and transition state theory. Catalysis, reaction rates and
thermodynamics of reaction. Catalytic power and specificity of enzymes (concept of active
site), Fischer’s lock and key hypothesis, Koshland’s induced fit hypothesis.
UNIT II: Enzyme kinetics No. of hours: 12
Relationship between initial velocity and substrate concentration, equilibrium constant, steady
state kinetics, mono-substrate reactions. Michaelis-Menten equation, Lineweaver-Burk plot,
29
Eadie-Hofstee and Hanes plot. Determination of KM and Vmax, Kcat, specificity constant. Effect
of pH and temperature on the activity of enzymes. Types of bisubstrate reactions (sequential –
ordered and random, ping pong reactions), examples. Differentiating bi-substrate mechanisms
(diagnostic plots, isotope exchange).
UNIT III: Enzyme inhibition No. of hours: 8
Reversible inhibition (competitive, uncompetitive, non-competitive and mixed) and

irreversible inhibition. Substrate inhibition. Structural analogs (allopurinol, methotrexate and
trimethoprim). Mechanism based inhibitors (β-lactam antibiotics, difluoromethyl ornithine),
clinical importance of enzyme inhibitors.
UNIT IV: Mechanism of action of enzymes No. of hours: 12
General features - proximity and orientation, strain and distortion, acid-base and covalent
catalysis (chymotrypsin, lysozyme). Metal activated enzymes and metalloenzymes, transition
state analogues. Coenzymes in enzyme catalyzed reactions. Structure, vitamin precursors,
types of reaction involved in: TPP, FAD, NAD, pyridoxal phosphate, biotin, coenzyme A,
tetrahydrofolate and lipoic acid.
UNIT V: Regulation of enzyme activity No. of hours: 10
Control of activities of single enzymes and metabolic pathways, feedback inhibition, allosteric
modulation (aspartate transcarbamoylase), regulation by reversible covalent modification
(glycogen phosphorylase and glycogen synthase). Proteolytic cleavage (zymogens-
chymotrypsinogen, trypsinogen, procaspases). Regulation of multi-enzyme complex,
properties (pyruvate dehydrogenase). Isoenzymes - properties and physiological significance
(lactate dehydrogenase, hexokinase and glucokinase).
UNIT VI: Applications of enzymes No. of hours: 10
Enzymes as reagents (glucose oxidase, cholesterol oxidase);Marker enzymes in diagnostics

(SGPT, SGOT, creatine kinase, alkaline and acid phosphatases);Enzyme linked immunoassay
(ALP and HRP);Enzyme therapy (streptokinase);Enzymes in research (Taq polymerase,
restriction endonucleases). Immobilized enzymes and industrial applications of enzymes.
PRACTICALS
1. Partial purification of an enzyme using bulk methods or chromatography

2. Assay to determine activity and specific activity of an enzyme
3. Progress curve for an enzyme
4. Effect of pH/temperature on enzyme activity
5. Determination of KM and Vmax of an enzyme using Lineweaver-Burk plot
6. Calculation of inhibitory constant (Ki) for an enzyme
7. Continuous assay of an enzyme
30
2.3 References
46412611-9.
2. Nicholas, C.P., Lewis, S. (1999). Fundamentals of Enzymology (3rd ed.). New York ,
Oxford University Press Inc. ISBN:0 19 850229 X.
3. Stryer, L., Berg, J., Tymoczko, J., Gatto, G. (2019). Biochemistry (9th ed.). New York,
WH: Freeman. ISBN-13: 9781319114671
1. Voet, D., Voet. J. G. (2013). Biochemistry (4th ed.). New Jersey, John Wiley & Sons
Asia Pvt. Ltd. ISBN : 978-1-11809244-6.

I Knowledge about the Historical perspectives; Oral questions will be
basic properties and Power point asked in the class.
characteristics of presentations; Teaching Assignments to classify
enzymes and their using chalk and board enzymes, determine
action; insights into the method. specific activity and
factors affecting enzyme reaction rates.
activity.
II Students will learn about Power point Class test will be
the kinetics of enzyme presentations; Teaching conducted for internal
catalyzed reactions and using chalk and board; assessment; Numerical
bisubstrate reactions Oral discussion sessions problems assigned for
in the class; Recent enzyme kinetics.
papers will be discussed
III Outline of the inhibitors Significance of inhibitors Various analytical
of enzymes and their will be discussed with problems will be assigned
clinical importance. use of research papers; to students related to
Classical chalk and board enzyme inhibition.
teaching and power point Students will identify
presentations examples of inhibitors of
various kinds.
IV Understanding of the Power point Demonstration by students
mechanism of enzyme presentations; Teaching with the help of models to
action and the role of using chalk and board; test their understanding.
coenzymes in catalysis. Oral discussion sessions
in the class
31
V Students will learn how Teaching using chalk and Problems will be assigned
enzymes are regulated board method along with to test student’s analytical
and the importance of power point presentations ability. Class tests will be
enzyme regulation in the and video tutorials. conducted for internal
cellular context. assessment. Students will
discuss methods of
regulation in groups.
VI Detailed knowledge of Teaching using chalk and Assignment of a small
the various applications board; Oral discussion project on identifying a
of enzymes in medicine sessions in the class; specific application of any
and research. Videos. Special lecture enzyme and tracings its
will be arranged on development and current
current status of use.
applications of enzymes
4. Keyword
Enzymes, Catalysis, Specific activity, Mechanism of action, Vitamins, Isoenzymes
32
CORE PAPER
Metabolism of Carbohydrates and Lipids (BCH C-5)
Semester - III
1. Course Objective
The objective of this course is to provide an understanding of metabolism of

carbohydrates and lipids, the enzymes involved in various metabolic pathways and regulation
of metabolism in cells. The course also aims to outline the importance of such pathways in
relation to metabolic defects.
The learners will be able to:
 Understand the concepts of metabolism, characteristics of metabolic pathways and

strategies used to study these pathways.
 Gain a detailed knowledge of various catabolic and anabolic pathways
 Understand the regulation of various pathways
 Gain knowledge about the diseases caused by defects in metabolism with emphasis on
the metabolic control
2.2 Course Contents
THEORY
UNIT I: Glycolysis, and pentose phosphate pathway No of hours: 12
Autotrophs, Heterotrophs, catabolism, anabolism, metabolic pathways, ATP as energy

currency, experimental approaches to study metabolism, High energy compounds. Glycolysis:
overview, reactions, regulations including hormones, fates of pyruvate, feeder pathways for
glycolysis, galactosemia. Lactose intolerance. Cori and Cori cycle. Pentose phosphate pathway
and its importance, Relationship between glycolysis and pentose phosphate pathway.
Anaerobic ATP production, fermentation.
UNIT II: Additional pathways in carbohydrate metabolism No of hours: 12
Glycogen synthesis, glycogen breakdown, regulation of glycogen metabolism,

gluconeogenesis. Glycogen storage diseases; Von Gierke, Pompe, Cori and McArdle.
Gluconeogenesis. Photosynthesis dark reaction: Calvin cycle, regulation, Photo respiration, C4
and CAM pathways in plants.
33
UNIT III: Citric acid cycle No of hours: 10
Overview of citric acid cycle, synthesis of acetyl Coenzyme A, enzymes of citric acid cycle,
regulation of citric acid cycle, anaplerotic reactions, amphibolic nature, Malate aspartate
shuttle, Glyceraldehyde-3-phosphate dehydrogenase shuttle, Glyoxylate cycle in plants.
Signaling pathways, regulation of carbohydrate metabolism by hormones, diseases associated
with metabolic irregularities.
UNIT IV: Degradation of lipids No of hours: 10
Lipid digestion, absorption and transport. Fatty acid oxidation: transport to mitochondria,
activation of fatty acids, β oxidation of saturated, unsaturated, odd and even numbered and
branched chain fatty acids, regulation of fatty acid oxidation, peroxisomal β oxidation, ω
oxidation and α oxidation. Ketone-body metabolism.
UNIT V: Synthesis of lipids No of hours: 10
Transport of mitochondrial Acetyl Co A to cytosol, Fatty acid synthase complex enzyme.

Synthesis of saturated, unsaturated, odd and even chain fatty acids, regulation of fatty acid
metabolism. Synthesis of glycerophospholipids and sphingolipids. Cholesterol metabolism,
diseases associated with abnormal lipid metabolism.
UNIT VI: Regulation of metabolism No of hours: 06
Well-fed state, early fasting state, fasting state, early re-fed state, energy requirements, reserves
and caloric homeostasis.
PRACTICALS
CREDIT : 2 TOTAL HOURS : 60
1. Estimation of blood glucose in serum using ortho toluidine method/ GOD-PxD

method
2. Sugar fermentation by microorganisms.
3. Assay of salivary amylase.
4. Isolation of lipids from egg yolk and separation by TLC.
5. Cholesterol estimation.
2.3 References
1. Devlin, T.M. (2011). Textbook of Biochemistry with Clinical Correlations (7thed.).

New York, John Wiley & Sons, Inc. ISBN:978-0-470-28173-4.
2. Nelson, D.L., Cox, M.M. (2017). Lehninger: Principles of Biochemistry (7thed.). New
46412611-9.
3. Voet, D., Voet. J. G. (2013). Biochemistry (4thed.). New Jersey, John Wiley & Sons
Asia Pvt. Ltd. ISBN:978-1-11809244-6.
34

I. Students will learn Traditional chalk and black Assignment, unit -test and
the concepts of board method, Audio visual practical assessment
metabolism with an presentation. Class room through experiment
emphasis on discussion
glycolysis and
gluconeogenesis
II. Students will learn Traditional chalk and black MCQ based assignments,
about glycogen board method with examples unit –test and practical
synthesis, and reactions and experiments assessment through
breakdown, glycogen experiment
storage diseases,
Calvin cycle C3 and
C4 pathways in
plants
III. The students will Revision of the previous Internal assessment tests
learn about classes will be conducted. will be conducted, –
overview, enzymes Traditional chalk and black presentations will be
and regulation of board method, Audio visual assessed along with
citric acid cycle and presentation practical assessment
glyoxylate cycle in
plants. They will
also learn about
hormonal regulation
of carbohydrate
metabolism and
diseases associated
with metabolic
irregularities.
IV The students will Chalk and board teaching Assessment through
learn about lipid along with presentations. Class midterm examination and
digestion, Fatty acid discussions on syllabus topics internal assessment test
oxidation, will be performed.
and Ketone-body
metabolism.
V. The students will Presentations will be delivered MCQ based internal
learn about synthesis along with traditional chalk assessment test will be
of saturated, board method. Class room held, quiz will be
unsaturated, odd and revisions will be conducted conducted and end term
even chain fatty before each class. examination.
acids and regulation
of fatty acid
metabolism. They
will also learn about
the synthesis of
35
glycerophospholipids
and sphingolipids.
Cholesterol
metabolism, diseases
associated with
abnormal lipid
metabolism
VI. The students will Traditional chalk and black End term examination
learn Well-fed state, board method, students will be evaluation, class room
early fasting state, asked to deliver seminars to quiz will be held, unit -
fasting state, early enhance their understanding test and practical
re-fed state in and presentation skills. assessment through
metabolism. experiment.
4. Keywords
Metabolism, Carbohydrates, Lipids, Glycolysis, Citric acid cycle, Allosteric regulation,

Fatty acid oxidation, Ketone bodies, Starve feed cycle, Blood glucose regulation
36
CORE PAPER
Membrane Biology and Bioenergetics (BCH C-6)
Semester III
1. Course Objective
The objective of the course is to provide students with the basic understanding of
membrane composition, structure-function relationship and properties of membranes. The
course will also provide an understanding of the various types of membrane transporters and
their molecular mechanisms. The course will introduce students to the basic tenets of
Bioenergetics and detail out the molecular mechanisms of oxidative phosphorylation and
photophosphorylation.
On successful completion of the course, students will:
 Understand the general composition and structure of biomembranes.

 Gain knowledge of the basic properties of membranes such as membrane fluidity.
 Have knowledge about the various types of membrane transport mechanisms.
 Understand the basic tenets of Bioenergetics.
 Be able to imbibe the concept of chemi-osmotic theory and the mechanism of oxidative
phosphorylation and ATP synthesis.
 Understand the basic mechanisms of photophosphorylation in plants and microbes.
2.2 Course Contents
THEORY
UNIT I: Membrane composition and structure No. of hours: 12
Historical background and various membrane models. Overview of membrane functions.

Composition of membranes: Lipids -Phospholipids, Glycolipids, sterols; Proteins - Peripheral
Proteins, Integral Membrane Proteins and Lipid-Anchored proteins, and carbohydrates.
Comparison of the composition of various cellular and subcellular membranes. Lateral and
transverse asymmetry in membranes. Role of Flippase, Floppase and Scramblase. Model
systems to study membranes - Lipid Monolayers, Planar Bilayer and Liposome, and their
application. Polymorphic Lipid-Water Systems. The various determinants of polymorphic
phases: CMC, lipid shape, critical packing parameter.
UNIT II: Membrane dynamics No. of hours: 8
Membrane fluidity: lateral, transverse and rotational motion of lipids and proteins. Factors
affecting membrane fluidity- composition, barriers (tight junctions), cytoskeleton interactions,
microdomains – rafts, caveolae. Fence and gate model. Study of RBC membrane architecture.
Homeoviscous Adaptation. Techniques to study membrane dynamics: FRAP, TNBS, SPT.
37
UNIT III: Membrane transport No. of hours: 12
Thermodynamics of transport. Simple diffusion and facilitated diffusion. Passive transport-

glucose transporter and anion transporter. Primary active transporters- P type ATPases, V type
ATPases, F type ATPases. Secondary active transporters - lactose permease, Na+ -glucose
symporter. ABC family of transporters – MDR and CFTR. Group translocation and
bacteriorhodopsin. Ion channels: voltage-gated ion channels (Na+ /K+ voltage-gated channel)
and ligand-gated ion channels (acetyl choline receptor), and aquaporins. Ionophores:
valinomycin, gramicidin. Relationship of membrane transport and diseases.
UNIT IV: Introduction to Bioenergetics No. of hours: 8
Laws of thermodynamics. Concept of state functions, free energy change, equilibrium constant,
coupled reactions, energy charge, ATP cycle, phosphorylation potential, and phosphoryl group
transfers. Chemical basis of high standard energy of hydrolysis of ATP, PEP, 1,3 BPG and
thioesters. Redox reactions, standard redox potentials and Nernst equation. Universal electron
carriers.
UNIT V: Oxidative phosphorylation No. of hours: 10
The electron transport chain - its organization and function. Peter Mitchell’s chemiosmotic
hypothesis and Proton motive force. FoF1 ATP synthase, structure and mechanism of ATP
synthesis. Metabolite transporters in mitochondria. Regulation of oxidative phosphorylation.
ROS production and antioxidant mechanisms. Thermogenesis Alternative respiratory
pathways in plants.
UNIT VI: Photophosphorylation No. of hours: 10
General features of photophosphorylation, historical background and Hill’s reaction. Role of

photosynthetic pigments and light harvesting systems in plants and microbes. Bacterial
photophosphorylation in purple bacteria and Green sulfur bacteria. Photophosphorylation in
plants. Molecular architecture of Photosystem I and Photosystem II. The Z-scheme of
photosynthetic electron flow. Cyclic photophosphorylation and its significance.
PRACTICALS
CREDIT: 2 TOTAL HOURS: 60
1. Effect of lipid composition on the permeability of a lipid monolayer.

2. Determination of CMC of detergents.
3. Preparation of RBC ghost cell.
4. Study the photosynthetic O2 evolution in hydrilla plant.
5. Isolation of chloroplast from spinach leaves and estimation of chlorophyll content.
6. Study the Hill reaction by using artificial electron acceptor.
7. Separation of photosynthetic pigments by TLC.
8. Separation of RBC membrane proteins by SDS-PAGE.
9. Isolation of mitochondria from liver and assay of marker enzyme SDH.
38
2.3 References
1. Garret, R.H., Grisham, C.M. (2016). Biochemistry (6th ed.). Boston, Cengage Learning.
ISBN-10: 1133106293, ISBN-13: 978-1133106296
2. Lodish, H., Berk, A., Kaiser, C.A., Krieger, M., Bretscher, A., Ploegh, H., Amon, A.,
Scott, M.P. (2016). Molecular Cell Biology (8th ed.). New York, WH: Freeman &
Company. ISBN-13: 978-1-4641-0981-2.
6412611-9.
4. Voet, D.J., Voet, J.G., Pratt, C.W. (2008). Principles of Biochemistry (3rd ed.). New
York, John Wiley & Sons, Inc. ISBN:13: 978-0470-23396-2
1. Wardhan, R., Mudgal, P. (2017). Text Book on Membrane Biology (1st ed.). Singapore,
Springer. ISBN-10: 9811071004, ISBN-13: 978-9811071003

I. Understand the Traditional chalk & board Post lecture students will
general composition method with powerpoint be given home
and structure of presentations. assignments to enhance
biomembranes. To their learning and for
study various Students to do comparative assimilation of concepts.
membrane model study of various cellular and Prelecture quiz to evaluate
systems and their subcellular membranes. students understanding of
application. previous lecture.
II. Understand Traditional chalk & board Post lecture students will
membrane fluidity, method with powerpoint be given home
and various presentations assignments to enhance
techniques used to their learning and for
study membrane assimilation of concepts.
fluidity. Prelecture quiz to evaluate
students understanding of
previous lecture.
III. Have knowledge Traditional chalk & board Post lecture students will
about the various method with powerpoint be given home
types of membrane presentations. assignments to enhance
transport their learning and for
mechanisms. assimilation of concepts.
Prelecture quiz to evaluate
previous lecture.
Mid-term exam.
39
IV Understand the basic Traditional chalk & board Post lecture students will
tenets of method with powerpoint be given home
Bioenergetics. presentations. Numerical assignments to enhance
problems relating to free their learning and for
energy change, entropy, etc., assimilation of concepts.
to be done in class to explain Prelecture quiz to evaluate
spontaneous, endothermic, students understanding of
exothermic reactions. previous lecture.
V. Understand the Traditional chalk & board Post lecture students will
concept of method with powerpoint be given home
chemiosmotic theory presentations. assignments to enhance
and the mechanism Numerical problems relating their learning and for
of Oxidative to standard redox potential, assimilation of concepts.
phosphorylation and proton motive force done in Prelecture quiz to evaluate
ATP synthesis. class. students understanding of
Videos of rotational catalysis previous lecture.
shown.
VI. Traditional chalk & board Post lecture students will
Understand the basic method with powerpoint be given home
mechanisms of presentations. Numerical assignments to enhance
photophosphorylation problems relating to their learning and for
in plants and photophoshorylation assimilation of concepts.
microbes. efficiency done. Prelecture quiz to evaluate
previous lecture.
Power point presentation
by students.
4. Keywords
Membrane asymmetry, Membrane fluidity, ATPase, Ion channels, Ionophores, PMF,

Oxidative phosphorylation, Photophosphorylation.
40
CORE PAPER
Hormone : Biochemistry and Function (BCH C-7)
Semester - III
The course is designed to provide an understanding of the process of cellular

communication including signal reception, transduction, amplification and response. The
course will enable students to understand and appreciate the delicate network and balance of
hormones required for the healthy functioning of the human body. It will provide an
understanding of the different endocrine factors that regulate metabolism, growth, ionic
homeostasis, glucose homeostasis and reproductive function. It outlines the consequences of
hormonal imbalances with special emphasis on human diseases. The course will also prepare
a student for postgraduate studies in any course related to molecular medicine.
On successful completion of the course, a student will:
 Understand and appreciate the different cognate and non-cognate modes of

communication between cells in a multi-cellular organism
 Understand the role of endocrine system in maintaining ionic and glucose homeostasis
 Be able to describe molecular, biochemical and physiological effects of all hormones
and factors on cells and tissues.
 Understand the integrative communications that regulate, growth, appetite, metabolism
and reproduction\
 Be prepared for interpreting clinical parameters in a real life situation
2.2 Course Contents
THEORY
UNIT I: Introduction to Endocrinology and Cellular signaling No of hours: 17
Functions of hormones and their regulation. Chemical signaling - endocrine, paracrine,

autocrine, intracrine and neuroendocrine mechanisms. Chemical classification of hormones,
transport of hormones in the circulation and their half-lives. Hormone therapy. General
introduction to Endocrine methodology. Hormone receptors - extracellular and
intracellular. Receptor - hormone binding, Scatchard analysis. G protein coupled receptors, G
proteins, second messengers - cAMP, cGMP, IP3, DAG, Ca2+, Effector systems - adenylyl
cyclase, guanylyl cyclase, PDE, PLC. Protein kinases (PKA, PKB, PKC, PKG). Receptor
tyrosine kinases - EGF, insulin and Ras - MAP kinase cascade. Non receptor tyrosine kinase-
erythropoietin receptor JAK - STAT pathway. Steroid hormone Receptor. Receptor
regulation and cross talk.
41
UNIT II: Hypothalamic- Hypophysial system: No. of hours: 5
Hypothalamic - Pituitary axis: anatomy, histology, vasculature and secretions. Physiological

and biochemical actions of hypothalamic hormones and anterior pituitary hormones; Hormone
feedback regulatory cascade. Posterior pituitary hormones –structure, physiology and
biochemical actions of AVP and Oxytocin; Diabetes insipidus.
UNIT III: Hormones regulating Metabolism, Calcium homeostasis and Growth:

No. of hours: 14
Thyroid gland - Histology; Biosynthesis of thyroid hormone and its regulation: Role of TRH
and TSH in T4 synthesis and response. Physiological and biochemical action of Thyroxine.
Pathophysiology of thyroxine secretion: Hyper and hypothyroidism, Goiter, Graves’ disease,
Cretinism, Myxoedema.
Regulation of calcium homeostasis: PTH, Vitamin D and calcitonin. Mechanism of Ca2+
regulation and pathways involving bone, skin, liver, gut and kidneys. Pathophysiology - rickets,
osteomalacia, osteoporosis.
Regulation of Growth: growth hormone and somatomedin, Endocrine disorders - gigantism,
acromegaly, dwarfism, pygmies. Physiology and biochemical actions of Growth factors- EGF,
PDGF and Erythropoietin.
UNIT IV: Hormones of the Adrenals: No. of hours: 8
Histology of Adrenal Gland. Physiology and action of Aldosterone; the Renin Angiotensin
System. Physiology and Biochemical actions of Cortisol. Regulation of cortisol synthesis:
POMC and CRH. Adrenal medullary Hormones: Epinephrine and Norepinephrine. The Fight
or flight response; Dual receptor hypothesis. General adaptation syndrome: acute and chronic
stress response. Pathophysiology – Addison’s disease, Conn’s syndrome, Cushing
syndrome.
UNIT V: Pancreatic and GI Tract Hormones: No. of hours: 10
Cells involved in the release of gastrointestinal hormones; the gastrin family of hormones and
CCK: the secretin family of hormones; Incretins; Ghrelin; Summary of hormone metabolite
control of GI function. Hormones of the Pancreas: Structure, synthesis, physiology and
biochemical actions of insulin and glucagon. Adipocyte hormones: Adiponectin and leptin;
Appetite and satiety control. Pathophysiology - Type I and type II Diabetes mellitus.
UNIT VI: Reproductive Hormones: No. of hours: 6
Male and female sex hormones. Interplay of hormones during ovarian and uterine phases of
menstrual cycle; Placental hormones; role of hormones during parturition and
lactation. Hormone based contraception and hormone therapy.
PRACTICALS
CREDIT: 2 TOTAL HOURS : 60
1. Determination of oral Glucose tolerance test as a confirmatory test for Diabetes

Mellitus.
42
2. Estimation of serum Ca2+.
3. Estimation of serum T4
4. HCG based pregnancy detection test.
5. Estimation of serum electrolytes.
6. Case studies on hormone disorders.
2.3 References
1. Cooper, G.M., Hausman, R.E. (2009). The Cell: A Molecular Approach (5th
ed.). Washington, DC: ASM Press & Sunderland, Sinauer Associates. ISBN:978-0-
87893-300
2. Hadley, M.C., Levine, J.E. (2007). Endocrinology (6th ed.). New Delhi, Pearson
Education, Inc. ISBN: 978-81-317-2610-5.
46412611-9.
4. Widmaier, E.P., Raff, H., Strang, K.T. (2019). Vander’s Human Physiology (15th ed.).
USA, McGraw Hill International Publications. ISBN: 978-0-07-128366-3.
Unit Course Learning Outcomes Teaching and Learning Assessment Tasks

No. Activity
I. Students will be introduced to Teaching will be Students will be given
hormones, various types of conducted both through questions that are
cellular signaling, classical black board mode and application based and
and modern endocrine power point presentation require analytical
methodologies. They will mode. skills. Quizzes will be
understand the concept of held to gauge their
signal, reception, conceptual
transduction, amplification understanding.
and response, Scatchard
analysis, signal transduction
and steroid receptors.
II. They will also gain insight Powerpoint presentations Oral questions will be
into significance of the and black board and oral asked in the class.
hypothalamic pituitary axis, discussions will be used
secretions of the for teaching Students will be given
hypothalamus, anterior and to prepare power point
posterior pituitary, concept of presentation on the
hormonal feedback assigned topics related
regulation. to the class teachings.
III. Knowledge about the Classical chalk and board Students will be asked
synthesis, structure and teaching, oral discussions to analyze case
biochemical functions of the and power point studies. Open book
thyroid gland secretions, presentation whenever tests will be held to
factors that monitor calcium needed. promote self-learning.
homeostasis in the human Practical related oral
43
body and hormonal networks Practical analysis of serum questions will be
that regulate growth and samples for understanding asked.
repair. diagnosis of thyroid
hormone pathophysiology
and imbalances in calcium
homeostasis.
IV Appreciate the significance of Both black board mode
the adrenal histology with and power point Regular class
respect to synthesis of presentation mode will be question-answer
cortical and medullary used. sessions.
hormones. The concept of
blood pressure regulation and Students will be asked
electrolyte balance will be to prepare PowerPoint
understood. Role of presentation on any
medullary hormone topic of interest
epinephrine in fight and flight relating to hormone
response, general adaptation biochemistry.
syndrome and the
biochemical changes during Internal assessment
acute and chronic stress will tests will be
be learned. conducted.
V. Gain knowledge about Teaching will be Internal assessment
histology of gastrointestinal conducted both through tests will be
tract with respect to black board mode and conducted
regulation secretion of power point presentation Discussions using
gastrointestinal hormones, mode. case studies will be
regulation of satiety and conducted.
appetite. Other topics include Practical assessment of
glucose homeostasis and role glucose homeostasis by
of hormones and other factors RBG and GTT.
in the same. Students will get
an insight into dysregulations
that lead to pathophysiologies
like anorexia, bulimia,
diabetes, obesity and
metabolic syndrome.
Understand the role of sex Teaching will be Regular oral
VI. hormones, hormonal conducted through black evaluation will be
regulation of menstrual cycle, board and power point done. Internal
gestation, parturition and presentation. Useful video assessment tests will
lactation and hormonal clips will be shown for be conducted
contraception. better clarity.
4. Keywords
Cellular communication, signal transduction, hypothalamic-hypophysial axis,

hormones, calcium and glucose homeostasis, hormonal disorders.
44
CORE PAPERS
Human Physiology (BCH C-8)
Semester – IV
The objective of the course in human physiology is to provide a comprehensive study

of the molecular and cellular mechanisms that govern the integrative working and regulation
of the various organ systems in the human body. The course will provide a foundation of the
physiological principles and the application of the same in real-life situations. It also outlines
the factors and biochemical events that disrupt homeostasis leading to pathophysiology. The
course will prepare students for higher education in any field related to molecular medicine.
On successful completion of this core paper, students should be able to:
 Understand the basic organization and homeostatic control of the human body from the
cell itself to organ systems and the functioning of the whole body.
 Comprehend and appreciate the importance of the fluid components of the body in
regulating and connecting the various organ systems; particularly the heart and vascular
system.
 Appreciate and understand the biochemical, molecular and cellular events that
orchestrate the coordinate working of the organ systems that regulate life processes.
 Get a holistic understanding of the different organ systems with respect to their
basic functioning, which involves both integrative learning and the regulatory roles of
the Nervous and Endocrine system.
 Develop in students an inquisitive learning approach to seek answers regarding the
complex workings of brain.
 Understand the factors that cause an imbalance to the Homeostatic control in the body
and how these lead to disorders and diseases.
 Perform and analyze various physiological tests that examine the function of various
systems of the human body.
2.2 Course Contents
THEORY
UNIT I: Introduction to Human body and Understanding Homeostasis No. of hours: 3
Physiology: overview and definition, levels of structural organization, organ system. Body
fluid compartments: intracellular, extracellular and interstitial fluid. Homeostasis: definition
and control mechanisms (negative and positive feedback mechanisms).
45
UNIT II: Blood, Heart and Circulation: No. of hours: 16
Components of blood: Plasma - Composition, SPE - electrophoretic pattern of serum proteins,

major plasma proteins and their role, Erythrocytes- erythropoiesis, function and metabolism,
Leukocytes, Platelets- structure and function; Hemostasis and its molecular mechanism, role
of platelets in coagulation, role of vitamin K in coagulation, Anticlotting and fibrinolytic
systems. Anemias: definition and types (Hemolytic, hemorrhagic, megaloblast, pernicious, iron
deficiency and aplastic anemia), polycythemia, Hemophilia and Thrombosis.
Anatomy of heart. Automacity of the cardiac muscle conducting fibres; Physiology of cardiac
contracting muscle fibres, Relationship between cardiac cycle, heart sound, ventricular
volumes and the ECG. Control of Heart rate and stroke volume. The vascular system: Arteries,
arterial blood pressure and its measurement, Capillaries and bulk flow across the capillary
walls, Veins and determination of venous pressure. Regulation of systemic arterial pressure.
Long term and short-term regulation of cardiac efficiency and blood pressure. Hypertension,
congestive heart disease, atherosclerosis, Heart failure and myocardial infarction.
UNIT III: Life Processes: No. of hours: 22
Respiratory physiology - Organization of the pulmonary system, site of gas exchange, Ventilation
and lung mechanics. Inspiration, Expiration, Lung compliance and its determinants. Lung
Volumes and Capacities. Transport of oxygen and carbon dioxide in blood. Haldane and Bohr’s
effect. Transport of hydrogen ions between tissues and lungs. Control of respiration. Hering-
Breuer reflex. Asthma, Chronic Obstructive Pulmonary Disease (COPD), Hypoxia,
Emphysema. Renal physiology - Anatomy of the kidney and the nephron. Regulation of renal
blood flow. Cell biology of the Bowmans’ capsule. Physiology of glomerular filtration and
GFR. Tubular processing of the glomerular filtrate. Micturition. Regulation of ion and water
balance. Urine concentration: The counter current multiplier system. Blood buffer systems,
renal responses to acidosis and alkalosis. Assessment of kidney function. Glomerular nephritis.
Dialysis: Hemodialysis and peritoneal dialysis. Diuretics. Gastrointestinal and hepatic physiology
- Histology of the gastrointestinal tract. Propulsion and motility of food and digested material.
Enteric reflexes. Secretory functions of the gastrointestinal tract, digestion and absorption of
macronutrients and micronutrients. Peptic ulcer, Sprue, Celiac disease, IBD, regurgitation.
Anatomy of the hepatic lobule and blood flow into the liver. Formation and secretion of bile.
Enterohepatic cycle, detoxification in liver. Jaundice, liver cirrhosis and fatty liver.
UNIT IV: Muscle No. of hours: 04
Structure of Skeletal, smooth and cardiac muscle, Molecular mechanisms of skeletal muscle
contraction: role of troponin, tropomyosin, and calcium in contraction, excitation-contraction
coupling. Smooth muscle contraction and its control. Excitation-contraction coupling in
cardiac muscle.
UNIT V: Reproductive Physiology: No. of hours: 06
Sex determination and differentiation. Development of female and male genital tracts.
Oogenesis, Spermatogenesis, capacitation and transport of sperm, blood-testis barrier.
Fertilization. Early development, Implantation. Placentation and Parturition.
46
UNIT VI: Neurophysiology: No. of hours: 09
Central Nervous system. Peripheral Nervous system. Blood brain barrier and CSF. Structure
and maintenance of neurons. Functional classes of neurons. Membrane potentials: Resting
Membrane Potential, Graded potentials, Action potential. Synapse: excitatory and inhibitory.
Temporal and spatial summation. Neurotransmitters and neuromodulators (definition with
examples). Somatic sensation: definition and cellular pathways of pain transmission and
modulation. Physiology of EEG, sleep.
PRACTICALS
1. Hematology:
a. Determination of Packed Cell Volume, Bleeding Time and Clotting time.

b. Preparation of blood smear and estimation of differential leucocyte count.
c. Enumeration of Blood cells: RBC and WBC counting, Calculation of blood
Indices.
d. Estimation of hemoglobin
2. Determination of total iron binding capacity.
3. Pulmonary function tests, spirometry and measurement of blood pressure.
4. Separation of isoenzymes of LDH by electrophoresis.
5. Case studies: Renal clearance, ECG, LFT, EEG (any two)
2.3 References
1. Fox, S.I. (2018) Human Physiology 15th ed., McGraw Hill International Publications,
(New York) ISBN 978-1259864629.
2. Widmaier, E.P., Raff, H. and Strang, K.T. (2019) Vander’s Human Physiology 15th ed.,
McGraw Hill International Publications (New York), ISBN: 978-1259903885
1. Guyton, A.C. and Hall, J.E., (2016) Reed Textbook of Medical Physiology 13th ed.,
Elseviers India Pvt. Ltd. (New Delhi). ISBN: 978-1455770052
2. Sherwood, L. (2012) Introduction to Human Physiology 8th edition; Brooks/Cole,
Cengage Learning. ISBN-13: 978-1133104544.

No. Activity
I. Understanding the concept of Teaching will be conducted Internal assessment
homeostasis and the both through black board tests;
mechanism for maintaining it; mode and power point Students will be
Learning the importance of presentation mode; Using given questions that
different fluid components in online data to discuss the are application based
47
the human body; importance of fluid and require
Comparing the different compositions in diagnosis. analytical skills
extracellular fluids with respect
to composition and function.
II. Learning the importance of Teaching will be conducted Conduct of Internal
plasma compositional both through black board assessment tests
variations as an important mode and power point Case study with
diagnostic tool. Understanding presentation mode. hematological
the biochemistry and Hematological practical’s as reports.
physiological role of RBC. an important diagnostic tool
Learning the biochemistry of for anemias, infections and
blood coagulation and the bleeding disorders.
factors that lead to bleeding and
coagulation pathopysiologies.
Understand the anatomy,
physiology and biochemistry of
cardiac function. Understand
the biophysics of movement of
blood through the vasculature.
Discuss and appreciate the
factors that lead to
pathophysiology of the
cardiovascular system.
III. Learning the anatomy, Teaching will be conducted Internal assessment
physiology and biochemistry of both through black board tests will be
pulmonary respiration and mode and power point conducted
transport of oxygen for cellular presentation mode. Analyzing case
Discussions with case studies studies.
utilization. Understand the
and quizzes will be conducted Open book tests to
importance of renal excretion to keep the students up-to-date promote self-
of nitrogenous wasted by with the information they have
learning the process of urine learning.
received and to gauge their
formation. Understand the conceptual understanding
process of ingestion, digestion
and assimilation of food. Learn
to correlate biochemical
mechanism to the manifestation
of symptoms associated with
the pathophysiologies related
with the three important life
processes- respiration,
digestion and excretion.
IV Understanding the biochemical Teaching will be conducted Internal assessment
mechanism that underlie the both through black board tests will be
contraction of skeletal muscles. mode and power point conducted
Comparing the differences in presentation mode.
smooth, skeletal and cardiac .
muscle with respect to anatomy
mechanism of contraction and
regulation.
48
V. Comparing the cell biology and Teaching will be conducted Internal assessment
physiology of spermatogenesis both through black board tests will be
versus oogenesis. mode and power point conducted.
Understanding the mechanism presentation mode. Analysis of case
that define, spermatogenesis, Discussions using case studies studies.
will be conducted.
spermiogenesis, semen
composition and capacitation.
Learning the process of cellular
development that support and
regulate oogenesis.
Understanding acrosomal
reaction, cortical response and
polyspermy that ensure proper
fertilization. Understanding the
physiological processes
involved in implantation,
placentation and parturition
VI. Understand the cellular Teaching will be conducted Internal assessment
composition and anatomy of both through black board tests will be
the central and peripheral mode and power point conducted
nervous system. Learning the presentation mode. A PowerPoint
process of synthesis, presentation on
composition and function of any topic of
CSF. Understand the interest relating to
mechanism of generation, Neurophysiology
propogation and regulation of and chemistry.
action potentials. Learning
about the neurophysiology and
chemistry of sensory
perception, learning and
memory and sleep.
4. Key words
Physiology, Homeostasis, life processes, heart, neurophysiology, reproduction
49
CORE PAPER
Gene Organization, Replication and Repair (BCH C-9)
Semester - IV
The objective of the course is to introduce to the students, the basic concepts of genome,
DNA structure, genes, chromatin and chromosomes. It provides comprehensive understanding
of DNA replication, recombination, mutations and repair processes in a way that students can
apply this knowledge in understanding the life processes and develop an interest to pursue high
quality research.
 Students will acquire basic information about the structure of DNA and various forms
of DNA, about organization of genome in various life forms, supercoiling of DNA and
its significance
 Students will learn about the molecular basis of processes like DNA replication,
recombination and transposition and understand the significance of these processes
 Students will learn about the various ways in which the DNA can be damaged leading
to mutations and lesions and different ways to repair DNA damage
2.2 Course Contents
THEORY
CREDIT : 4 TOTAL HOURS: 60
UNIT I: Structure of DNA No. of hours: 10
Building blocks of DNA structure, Watson and Crick model, features of the double helix,
various forms of DNA, denaturation and renaturation of DNA, hyperchromicity, melting
temperature, factors affecting Tm of DNA molecules. Supercoiling of DNA, linking number,
topoisomerases and their classification. Topoisomerase inhibitors and their clinical importance.
UNIT II: Genes and genomic organization No. of hours: 10
Definition of a gene, organization of genes in viruses, bacteria and eukaryotes, concept of split
genes, introns, exons, satellite DNA, highly repetitive DNA, centromere and telomere
sequences. Nucleosome structure and packaging of DNA into higher order structures.
UNIT III: Replication of DNA No. of hours: 16
General features of replication, the chemistry of DNA synthesis, DNA polymerase, the
replication fork, enzymes and proteins in DNA replication, E coli DNA polymerases, stages of
replication-initiation, elongation and termination, origin of replication, relationship between
replication and cell division, replication in eukaryotes, end replication problem, telomerase,
50
various modes of replication. Comparison of replication in prokaryotes and eukaryotes.
Inhibitors of DNA replication and applications in medicine.
UNIT IV: Recombination and transposition of DNA No. of hours: 12
Homologous recombination, biological role and models for homologous recombination,

proteins and enzymes in homologous recombination, site-specific recombination, serine and
tyrosine recombinases. Transposition, the three classes of transposable elements-DNA
transposons, virus-like retrotransposons and poly-A retrotransposons. DNA transposition by
cut and paste and replicative mechanism.
UNIT V: Molecular basis of mutations No. of hours : 6
Importance of mutations in evolution of species. Types of mutations - transition, transversion,

frame shift mutations. DNA damage by hydrolysis, alkylation, oxidation and radiation.
Mutations caused by base analogs and intercalating agents. Ames test.
UNIT VI: Various modes of DNA repair No. of hours : 6
Replication errors and their repair, mismatch repair system. Repair of DNA damage-direct
reversal of DNA damage, base excision repair, nucleotide excision repair, recombination
repair, trans-lesion DNA synthesis. DNA repair and diseases.
PRACTICALS
CREDITS : 2 TOTAL HOURS : 60
1. To hydrolyze DNA and separate nucleotide bases by paper chromatography

2. To plot ultraviolet absorption spectrum of DNA
3. Determination of DNA concentration by A260nm
4. DNA estimation by Diphenylamine (DPA) method
5. Determination of the melting temperature of DNA
6. Isolation of chromosomal DNA from E coli cells
2.3 References
1. Nelson, D.L. and Cox, M.M (2017) Lehninger: Principles of Biochemistry (7th
ed.) W.H. Freeman & Company (New York), ISBN:13: 9781464126116 / ISBN:10-
1464126119.
2. Watson, J.D., Baker, T.A., Bell, S.P., Gann, A., Levine, M. and Losick, R. (2008)
Watson: Molecular Biology of the Gene (7th ed.), Cold Spring Harbor Laboratory Press,
Cold spring Harbor (New York), ISBN:0-321-50781 / ISBN-13: 9780321762436
51

No. Activity
I. Students will learn about the Teaching using chalk and Oral questions will be
complexity of DNA double board; Power point asked in the class.
helix structure, nature of presentations; Oral discussion Problems will be
nuclotides, melting of DNA sessions in the class assigned to test
and understand the importance student’s analytical
Practical learning of ability. Asking
of supercoiling of DNA.
hydrolysis of DNA, separation practical related
of nucleotide bases using questions.
paper chromatography,
melting temperature of DNA.
II. Gain insight into the Power point presentations will Regular question-
organization of DNA and how be used to teach levels of answer sessions in the
a long DNA molecule gets DNA packaging ; Oral class. Class tests will
packaged in a small cell. discussion sessions in the be conducted for
class internal assessment
III. Understand the details of Teaching will be carried out Students will be
DNA replication and by displaying colourful challenged with
importance of various proteins models for steps of replication analytical problems,
and enzymes involved in using slides and the rest using puzzles and
replication and application of chalk and board method; assignments related to
Discussion sessions in the replication of DNA.
inhibitors class
IV Learn to appreciate the Power point presentations will Regular question-
mechanism and importance of be used to explain answer and quiz
homologous and site specific recombination process; sessions in the class,
recombination and Interactive discussion sessions demonstration by
transposition. in the class students with the help
of models to test and
improve their
understanding.
V Know about DNA mutations Teaching using chalk and Regular class
and understand how DNA can board; Power point interaction and
be damaged by chemical presentations; Oral discussion analytical problem
mutagens and radiation. sessions in the class solving in the class.
Class tests will be
conducted for internal
assessment
VI. Will be familiarized with Power point presentations as Various analytical
various strategies of DNA well as chalk and board problems will be
repair and diseases associated method will be used for assigned to students
with DNA repair problems. teaching, Oral discussion related to DNA repair
about repair and its problems and related disorders.
along with movie display.
4. Keywords
DNA, Double helix, Supercoiling, Recombination, Transposition, DNA Repair
52
CORE PAPER
Metabolism of Amino Acids and Nucleotides (BCH C-10)
Semester - IV
1. Course Objective
The main objective of the course is to offer detailed and comprehensive knowledge
about the synthesis and degradation pathways of amino acids and nucleotides and their
importance in the proper functioning of the cells. This course also interrelates the metabolism
of these molecules with respect to health diseases in addition to providing overview of
inhibitors of metabolism for treating the diseases of metabolic disorders.
At the end of the course the students will be able to:
 Extend their school level concepts of nitrogen cycle to understand the mechanism by
which nitrogen is fixed by microbes and how it’s incorporation in diet is critical to
human nutrition as well as comprehend the mechanism by which ammonia is
incorporated in biomolecules
 Systematically learn the breakdown and synthesis of amino acids and nucleotides in
humans and recognize its relevance with respect to nutrition and human diseases
 Gain knowledge of how amino acids are converted into a variety of precursors
 Acknowledge the role of inhibitors of nucleotide metabolism which are potentially
being used as chemotherapeutic drugs
 Comprehend how the amino acid and nucleotide metabolism are integrated with
carbohydrate and lipid metabolism
2.2 Course Contents
THEORY
UNIT I: Overview of Nitrogen and Amino Acid Metabolism No. of hours: 8
Nitrogen cycle, incorporation of ammonia into biomolecules. Digestion and absorption of

dietary proteins. Role of essential and non-essential amino acids in growth and development.
Protein calorie malnutrition - Kwashiorkar and Marasmus, Nitrogen balance. Metabolic fates
of amino groups. Transamination, role of pyridoxal phosphate, glucose-alanine cycle, Kreb’s
bicycle, urea cycle, its regulation and inherited defects of urea cycle. Gamaglutamyl cycle.
UNIT II: Catabolism and Biosynthesis of Amino Acids No. of hours: 18
Catabolic pathways of individual amino acids. Glucogenic and ketogenic amino acids.
Metabolism of one carbon units. Disorders of amino acids metabolism, phenylketonuria,
alkaptonuria, maple syrup urine disease, methyl malonic acidemia (MMA), homocystinuria
53
and Hartnup’s disease. Overview of amino acid synthesis. Biosynthesis of non-essential amino
acids and its regulation.
UNIT III: Precursor Functions of Amino Acids No. of hours: 8
Biosynthesis of creatine and creatinine, polyamines (putresine, spermine, spermidine),

catecholamines (dopamine, epinephrine, norepinephrine) and neurotransmitters (serotonin,
GABA). Porphyrin biosynthesis, catabolism and disorders of porphyrin metabolism.
UNIT IV: Biosynthesis, Degradation of Purine and Pyrimidine Nucleotides

No. of hours: 14
De novo synthesis of purine and pyrimidine nucleotides, regulation and salvage pathways.
Digestion of nucleic acids, degradation of purine and pyrimidine nucleotides. Inhibitors of
nucleotide metabolism. Disorders of purine and pyrimidine metabolism – Lesch-Nyhan
syndrome, Gout, SCID, adenosine deaminase deficiency.
UNIT V: Deoxyribonucleotides and Synthesis of Nucleotide Triphosphate and Co-

enzymes
No. of hours: 6
Biosynthesis of deoxyribonucleotides and its regulation, conversion to triphosphates,

biosynthesis of coenzyme nucleotides.
UNIT VI: Integration of Metabolism No. of hours: 6
Integration of metabolic pathways (carbohydrate, lipid and amino acid metabolic pathways),
tissue specific metabolism (brain, muscle, and liver).
Practical
PRACTICALS
1. Assay of serum transaminases – SGOT and SGPT.

2. Estimation of serum urea.
3. Estimation of serum uric acid.
4. Estimation of serum creatinine.
5. Estimation of bilirubin
6. Assay of glutamate dehydrogenase
2.3 References
1. Berg, J.M., Tymoczko, J.L. and Stryer L., (2012) W.H. Biochemistry (7th ed.), Freeman
and Company (New York), ISBN:10: 1-4292-2936-5, ISBN:13:978-1-4292-2936-4.
2. Devlin, T.M. (2011) Textbook of Biochemistry with Clinical Correlations (7th ed.), John
Wiley & Sons, Inc. (New York), ISBN:978-0-470-28173-4 / BRV ISBN:978-0-470-
60152-5.
1464126119.
54
Unit Course Learning Outcomes Teaching and Assessment

No. Learning Activity Tasks
I. Students will learn about the concepts of Students will be asked Internal
nitrogen cycle, nitrogen fixation and to orally revise the assessment
assimilation, importance of nitrogen in previous class before tests (midterm
human nutrition and its deficiency- every new class helping and end-term)
associated disorders. Besides, students will them in better will be
be introduced to metabolic fates of amino understanding and their conducted.
groups, various metabolic cycles, their doubts cleared, if any.
regulation and inherited defects of urea Teaching will be
cycle. conducted through both
black board mode and
powerpoint
presentation mode.
II. Students will gain insight into the Chalk and board Students will
breakdown and synthesis of amino acids. teaching method will be given
Further, the students will gain knowledge be largely employed. assignment on
about various disorders related to amino Oral presentations by different
acids. the students will help topics
them learn the subject specially
better. disorders and
will be asked
to deliver a
power-point
presentation
on the
assigned
topics.
III. Students will learn how amino acids are Class discussions will MCQ based
converted into a variety of precursors, such be conducted in Internal
as creatine and creatinine, polyamines various group of assessment
catecholamines, neurotransmitters and students. Lecture by test will be
porphyrin biosynthesis, catabolism and teachers. conducted.
disorders of porphyrin metabolism. Mid term
examination
evaluation.
IV Students will gain insight into de novo Oral questions will be Internal
synthesis and degradation of purine and asked by the teachers assessment
pyrimidine nucleotides, regulation and that will be orally test (end term)
salvage pathways. Further, the students will answered by the will be
learn about the inhibitors of nucleotide students. Chalk and conducted.
metabolism and disorders related to purine board teaching along Several short
and pyrimidine metabolism. with powerpoint quiz will be
presentations. held to
motivate
students
V. Students will gain knowledge about Students will be asked Students will
biosynthesis of deoxyribonucleotides, its to orally revise the be given
55
regulation and conversion to triphosphates, previous class before assignment on
Further they will also learn about the every new class. various topics
biosynthesis of coenzyme nucleotides. Student presentations and will be
and class discussions. asked to
deliver a
power-point
presentation
on the
assigned
topics. End
term
examination
evaluation
will be
conducted.
VI. Students will learn about Chalk and board Students will
the integration of various teaching method will be given
metabolic pathways and be largely employed. assignment on
their cross-talk in specific tissues like brain, Oral presentations by different
muscle, and liver. the students will help topics
them learn the subject specially
better. disorders and
will be asked
to deliver a
power-point
presentation
on the
assigned
topics.
4. Keywords
Nitrogen Balance, Protein calorie malnutrition, Transamination, Amino acid

metabolism, Purine and Pyrimidine Metabolism, Porphyrin metabolism, Urea cycle, Metabolic
disorders, Integration of metabolism
56
CORE PAPER
Concepts in Genetics (BCH C-11)
Semester – V
The aim of the course is to provide students with an understanding of both classical and
modern concepts in genetics with special emphasis on the areas of transmission genetics,
molecular and developmental genetics, mapping techniques, chromosomal aberrations and
population genetics. Students will gain a hands-on training experience of culturing and
conducting experiments on the genetic model system Drosophila melanogaster. The course
also works as preparation for further studies in a Master’s programme in molecular biology or
related topics.
On successful completion of the course, the students will be:
 Understanding the principles of Mendelian genetics, extensions and applications

 Learning and appreciating the various factors that confer genotypic and phenotypic
variability.
 Using the concepts of bacterial and viral genetics to understand resistance patterns and
to create linkage and genetic maps.
 Able to use statistical tools to analyze biological data.
 Able to apply the principles of transmission and inheritance in real life situations.
2.2 Course Contents
THEORY
UNIT I: Principles of heredity and transmission genetics: No of hours: 16
Mendelian genetics and chromosomal basis of heredity: Mendelian laws and ratios; Concept
of segregation and independent assortment, and its chromosomal basis. Laws of probability &
binomial expansion, formulating and testing genetic hypothesis, chromosomal basis of
Mendelism - Sutton and Boveri hypothesis with other supporting experimental evidences;
Extensions to Mendelian genetics: Complementation test using examples from Drosophila eye
colour mutants to differentiate allelic variants from gene interaction. Allelic variation and gene
function - dominance relationships, multiple alleles, lethal alleles and null alleles. Pleiotropic
gene interaction - epistatic and non- epistatic, interaction between gene(s) and environment.
Penetrance and expressivity, norm of reaction and phenocopy; Human pedigree analysis:
Pedigree conventions, characteristics of dominant and recessive inheritance; sex linked, sex
influenced and sex limited traits. Applications of pedigree analysis.
57
UNIT II: Genetics of bacteria and viruses No. of hours: 7
Concept of cistron. Bacterial and viral genomes, Mechanism of genetic exchange - conjugation,
transformation and transduction. Gene mapping in bacteria.
UNIT III: Linkage, crossing over and mapping techniques: No. of hours: 10
Linkage and crossing over, genetic mapping in eukaryotes, centromere mapping with ordered
tetrads, cytogenetic mapping with deletions and duplications in Drosophila, detection of linked
loci by pedigree analysis in humans, LOD score, somatic cell hybridization for positioning
genes on chromosomes and physical maps using molecular markers.
UNIT IV: Molecular genetics No. of hours: 12
Sex determination and genetic control of development: Genetic basis of sex determination in
Humans, Drosophila melanogaster and C. elegans. Drosophila development-maternal effect
genes, morphogens and zygotic genes; Genetic basis of flower development in Arabidopsis-
ABC model; Non-nuclear inheritance and Epigenetics: Extra nuclear inheritance, tests for
organelle heredity and maternal effect; Mechanism of dosage compensation; X chromosomal
inactivation in humans and Drosophila melanogaster. Epigenetic mechanisms of
transcriptional regulation. Monoallelic expressions and Genomic imprinting.
UNIT V: Chromosomal aberrations No. of hours: 7
Variations in chromosome number: aneuploidy and polyploidy. Variations in chromosome

structure- inversions, deletions, duplications and translocations.
UNIT VI: Quantitative, Population and Evolutionary Genetics No. of hours: 8
Inheritance of complex trait, analysis of quantitative traits, narrow and broad sense heritability,
quantitative trait loci (QTL) and their identification. Hybrid vigor. Hardy-Weinberg law,
predicting allele and genotype frequencies and exceptions to Hardy-Weinberg principle.
Molecular evolution - analysis of nucleotide and amino acid sequences, molecular phylogenies,
homologous sequences, phenotypic evolution and speciation.
PRACTICALS
1. Squash preparation of salivary glands of Dipteran larva to observe polytene

chromosomes.
2. Induction of polyploidy in onion roots.
3. Smear technique to demonstrate sex chromatin in buccal epithelial cells.
4. Monohybrid crosses in Drosophila for studying autosomal and sex linked inheritance.
5. PTC testing in a population and calculation of allelic and genotype frequencies.
6. Study of abnormal human karyotype and pedigrees (dry lab)
58
2.3 References
1. Griffiths, A.J.F, Wessler, S. R, Carroll, S. B. and Doebley, J. (2017) An Introduction to

Genetic Analysis, (11th ed.), W.H. Freeman & Company (New York), ISBN:
1464109486
2. Pierce, B.A. (2012) Genetics - A Conceptual Approach, (6h ed.), W.H. Freeman & Co.
(New York), ISBN:13:978-1-4292-7606-1 / ISBN:10:1-4292-7606-1.
3. Snustad, D.P. and Simmons, M.J. (2012) Genetics (6th ed.), John Wiley & Sons.
(Singapore), ISBN: 978-1-118-09242-2.

No. Activity
I. Understanding Mendel’s laws Students will be practically Students will be
and ratios; Understand shown examples from given questions
relationship between genetic crosses of different that are application
inheritance, generation of Drosophila eye colour based and require
variation and cell division; mutant strains for use of statistical
Relating genes to explaining complementation tools like
chromosomes- chromosomal test. Formulation and testing probability and
basis of heredity; Use of of genetic hypothesis will be chi-square analysis
statistical tools in testing explained using experiments and hypothesis
genetic hypothesis; with Drosophila crosses as testing for
Complementation test relating well as exemplary goodness of fit.
extensions to Mendelian ratios numerical problems.
due to allelic variations; Students will be encouraged
Understand gene interactions- to apply pedigree analysis in
both epistatic and non-epistatic; real life situations by
Concept of Penetrance, helping them make their
expressivity, phenocopy and own family pedigrees for
pleiotropy; Understanding how certain overt heritable
to draw a human pedigree chart physical features and
and analyze it for determining genetic condition or disease,
inheritance patterns if any.
II. Understand the concept of Teaching will be conducted Powerpoint
cistron, operon and gene; both through black board presentation on the
Basics of bacterial and viral mode and power point assigned topics.
genomes; Mechanisms of presentation mode. Students will be
genetic exchange in Discussions and quizzes given questions
prokaryotes like conjugation, will be conducted to keep that are application
transformation and the students up-to-date with based and require
transduction; the information they have analytical skills
Gene mapping in bacteria. received and to gauge their
conceptual understanding
III. Understand the of concept of Teaching will be conducted Internal
recombination and linked both through black board assessment tests
genes; Use recombination will be conducted
59
frequencies to determine gene mode and power point Questions on
order and distance; Genetic presentation mode. drawing a genetic
mapping in eukaryotes using Numerical problems for map with gene
test crosses; Gene to genetic mapping using three order, map
centromere mapping with point cross would be given distance. and
ordered tetrads and cytogenetic for practice in class. centromere
mapping; Detection of linked mapping
loci by pedigree analysis in
humans and the concept of
LOD score; Somatic cell
hybridization for locating gene
on a chromosome;
Physical mapping using
molecular markers.
IV Understand the difference in Teaching will be conducted A PowerPoint
the genetic basis of sex both through black board presentation on
determination in Humans, mode and power point any topic of
Drosophila and C.elegans; presentation mode. interest relating to
Understand the role of maternal Discussions and quizzes the concept of
effect genes on axis formation will be conducted to keep Epigenetics, non-
during development using the students up-to-date with nuclear inheritance
Drosophila as a model of study the information they have and sex
Role of zygotic and homeotic received and to gauge their determination.
genes in development using conceptual understanding
Drosophila as a model of
study; Genetic control of
flower development in
Arabidopsis; Nonnuclear
inheritance and its role in
determination of phenotypes;
Epigenetic phenomenon like
dosage compensation and
Genomic Imprinting.
V. Students will learn about Teaching will be conducted Internal
various structural and numeric both through black board assessment tests
chromosomal aberrations mode and power point will be conducted
possible in both plants and presentation mode. Analysis of case
animals; Understand the Discussions using case studies in groups.
disadvantages as well as some studies will be conducted to
advantages of such aberrations. help students understand the
karyotype analysis.
VI. Understand the concept of Teaching will be conducted Numerical analysis
polygenic inheritance, additive both through black board and case study
gene effect, OTL, heterosis and mode and power point analysis.
hybrid vigor; Understand presentation mode.
concept of gene pool, allelic Discussions using
and genotypic frequencies; population genetics based
Understand Hardy Weinberg case studies will be
principle and its limitations; conducted. Practical
Understand concept genetic collection of data from
60
drift, founder effect, genetic population to test Hardy-
bottleneck; Factors that Weinberg principle.
influence gene flow, fitness of
a population and speciation.
4. Keywords
Mendelian genetics, Allelic and gene interaction, Gene mapping, Microbial genetics,
Pedigree analysis, Epigenetics, Quantitative, Development, Population and Evolutionary
Genetics
61
CORE PAPER
Gene Expression and Regulation (BCH C-12)
Semester - V
1. Course Objective
The objective of the course is to introduce to the students the basic knowledge about
how genes are transcribed and how translation takes place in prokaryotes and eukaryotes and
how these processes are regulated, so that students can apply this knowledge in enhancing their
analytical and problem solving skills.
After completion of the course students will:
 acquire basic knowledge about the processes of transcription and translation in

prokaryotes and eukaryotes
 learn about the features of the genetic code and various experimental approaches used
to crack the code
 develop understanding of the molecular basis of RNA processing and RNA splicing
 learn about the various ways in which these biological processes are regulated and the
significance of regulation in maintaining life forms
2.2 Course Contents
THEORY
CREDIT : 4 TOTAL HOURS : 60
UNIT I: Transcription in prokaryotes No. of hours : 8
Comparison between transcription and DNA replication, RNA polymerases, transcription

cycle in bacteria, sigma factor, bacterial promoters, identification of DNA binding sites by
DNA footprinting, various stages of RNA synthesis, initiation, elongation and termination, rho-
dependent and rho-independent termination. Inhibitors of transcription and applications as
antimicrobial drugs.
UNIT II: Transcription in eukaryotes No. of hours : 8
Comparison between initiation, elongation and termination of prokaryotic and eukaryotic

transcription. Introduction on basal transcription machinery and three classes of eukaryotic
RNA polymerases – I, II and III and their respective promoters. Details on transcription by
RNA polymerase II, features of RNA polymerase II core promoters and general transcription
factors. Identification of DNA binding sites by DNA foot printing. Inhibitors of eukaryotic
transcription and their applications.
62
UNIT III: RNA Processing No. of hours : 8
Various types of RNA processing- polyadenylation and capping, processing of rRNA and
tRNA. Chemistry of RNA splicing, the spliceosome machinery, splicing pathways, group I and
group II introns, alternative splicing, exon shuffling and RNA editing.
UNIT IV: Translation of proteins No. of hours : 16
Salient features of the genetic code, triplet nature, degenerate, wobble in the anticodon.
Experimental approaches used to decipher the genetic code. Suppressor tRNAs. Exceptions to
the nearly universal genetic code. Messenger RNA, transfer RNA, charging of tRNA. The
structure of ribosome. Three stages of translation-initiation, elongation and termination.
Translation in eukaryotes. Regulation of translation. Comparison of prokaryotic and eukaryotic
protein synthesis. Inhibitors of translation and their clinical importance.
UNIT V: Regulation of gene expression in prokaryotes No. of hours : 10
Strategies for gene regulation, negative and positive regulation, concept of operons, regulatory
proteins, activators, repressors, DNA binding domains, regulation of lac operon and the
concept of combinatorial control, trp operon. Regulatory RNAs in bacteria, small RNA and
riboswitches.
UNIT VI: Regulation of gene expression in eukaryotes No. of hours : 10
Gene regulation by chromatin remodeling, regulation of galactose metabolism in yeast, action

Gof enhancers and insulators, working of activators and repressors, concept of combinatorial
control. Regulatory RNAs in eukaryotes: synthesis and mechanism of siRNA and miRNA.
Comparison of regulatory mechanisms of gene expression in prokaryotes and eukaryotes.
PRACTICALS
CREDITS : 2 TOTAL HOURS: 60
1. Estimation of RNA by Orcinol Method

2. Extraction of total nucleic acids from plant tissue
3. To study growth curve and diauxic growth curve effect in E. coli
4. Isolation of total RNA from bacteria/yeast
5. To study the effect of inhibitors on protein synthesis
2.3 References
1464126119.
2. Watson, J.D., Baker, T.A., Bell, S.P., Gann, A., Levine, M. and Losick, R. (2008)
Watson: Molecular Biology of the Gene (7th ed.), Cold Spring Harbor Laboratory Press,
Cold spring Harbor (New York), ISBN:0-321-50781 / ISBN-13: 9780321762436
1. Lewin, B., Krebs, J.E., Kilpatrick, S.T., Goldstein, E.S., (2018) Lewin’s Gene X
(10th edition). Bartlett Learning publishers, LLC, ISBN: 978-0-7637-6632-0.
63

I. The student will learn Traditional chalk and board Problem solving
about the difference method of teaching and regular assignments, regular
between DNA class room discussion. Videos question answer sessions,
replication and to showcase the structure and MCQs and unit-test for
transcription, RNA assembly of the transcription internal assessment
polymerases and initiation complex and the
details of bacterial stages of transcription in real
transcription time.
II. Will appreciate the Audio visual presentation with Regular question-answer
basics of prokaryotic appropriate examples and sessions in the class,
and eukaryotic black board teaching, regular learning exercises through
transcription, key class room discussion quiz and puzzles,
features of the three Estimation of RNA and analytical question solving
classes of eukaryotic isolation of RNA will be to improve student
RNA polymerases, shown through practicals. understanding.
different promoters Monitoring of practical
and use of various record keeping, oral
inhibitors. questions related to
practicals
III. Introduced to the Chalk and board method of Oral questions will be
ways of RNA teaching; Power point asked in the class.
processing, chemistry presentation showing the steps Problems will be assigned
of splicing, various of splicing and RNA editing to test student’s analytical
types of splicing and and various examples of ability.
RNA editing splicing.
IV Able to describe the Classroom teaching of Students will be

salient features of discoveries from research challenged with analytical
genetic code, triplet papers, chalk and board problems, puzzles and
nature, wobble in the method of teaching and use of assignments related to
anticodon. Stages of powerpoint presentation. genetic code and other
translation and Practical demonstration of topics covered in the class.
translation inhibitor.
inhibitors of translation
Audio visual to demonstrate
the experimental strategies
used to decipher the genetic
code
V. Gain knowledge Traditional chalk and board Various analytical
about regulation of method of teaching, audio problems will be assigned
gene expression in visual presentation and regular to students related to
prokaryotes, concept of class room discussion. prokaryotic gene
operon, regulatory Supportive powerpoint slides expression, oral question
RNA and riboswitches. to display the structure of answer sessions will be
riboswitches held in the class.
64
VI. Learn about regulation Classroom teaching using Regular classroom
of gene expression in powerpoint presentations along interaction and analytical
eukaryotes, working of with use of traditional chalk problem solving related to
activators and and board class room gene expression and
repressors and small discussion. audio visual aids to silencing. Class tests will
RNA mediated present RNA silencing be conducted for internal
silencing mechanisms. mechanisms assessment
4. Keywords
RNA, Transcription, Translation, Genetic code, Gene expression, Operon
65
CORE PAPER
Genetic Engineering and Biotechnology (BCH C-13)
Semester – VI
1. Course objectives:
The objective of the course is to teach the basics of theoretical and practical aspects of
recombinant DNA technology and various techniques for DNA manipulation in prokaryotes
and eukaryotes. Applications of these techniques in production of recombinant therapeutic
proteins and vaccines will also be outlined in this course.
2.1 Course Learning Outcome
The students will be able to understand:
 The process for isolation and engineering of DNA using restriction and modification
enzymes.
 Use of cloning and expression vectors.
 The methods for creation of genomic and cDNA libraries, their applications and use.
 Understanding the methods for protein production and their application in industrial
production systems.
2.2 Course Contents
THEORY
UNIT I: The basic principle of gene cloning No of hours: 10
Restriction and modification systems, restriction endonucleases and other enzymes used in
manipulating DNA molecules. Ligation of DNA molecules. DNA ligase, sticky ends, blunt
ends, linkers and adapters, homopolymer tailing, Synthetic oligonucleotides.
UNIT II: Cloning vectors for prokaryotes and eukaryotes No of hours: 12
Plasmids and bacteriophages as vectors for gene cloning. Cloning vectors based on E. coli
plasmids, pBR322, pUC8, pGEM3Z. Cloning vectors based on M13 and λ bacteriophage, and
in vitro packaging. Vectors for yeast, Ti-plasmid, and retroviral vectors, high capacity vectors
BAC and YAC.
UNIT III: Introduction of DNA in cells, selection for recombinants and clone
identification
No of hours: 10
Uptake of DNA by cells. Selection and identification for transformed cells, insertional
inactivation, blue-white selection. Transfection. Chemical and physical methods of DNA
introduction into cells. The problem of selection, direct selection, marker rescue. Identification
of recombinant phages, cDNA and Genomic libraries, identification of a clone from gene
66
library, colony and plaque hybridization probing, Southern and Northern hybridization,
methods based on detection of the translation product of the cloned gene.
UNIT IV: Expression of cloned genes No of hours: 06
Vectors for expression of foreign genes in E. coli, cassettes and gene fusions. Hybrid
promoters: trc, tac, pL and T7 promoter based expression vectors. Challenges in producing
recombinant protein in E. coli. Production of recombinant protein by eukaryotic cells. Fusion
tags such as, poly-histidine, glutathione, maltose binding protein and their role in purification
of recombinant proteins.
UNIT V: Polymerase chain reaction and DNA sequencing No of hours: 10
Fundamentals of polymerase chain reaction, Types of PCR; hot start, multiplex, reverse
transcriptase PCR and Nested PCR, quantitative PCR, Primer, designing for PCR. Cloning
PCR products. DNA sequencing by Sanger’s method including Automated Sanger’s DNA
sequencing. Introduction to Next Generation Sequencing.
UNIT VI: Applications of genetic engineering in Biotechnology No of hours: 12
Site–directed mutagenesis, Protein engineering (T4-lysozyme), yeast two hybrid systems,

Production of recombinant pharmaceuticals such as insulin, human growth hormone, factor
VIII. Recombinant vaccines. Gene therapy (SCID), Applications in agriculture – Bt cotton,
glyphosate herbicide resistant crops, ethical concerns.
PRACTICALS
1. Transformation of E. coli cells with plasmid DNA.

2. Isolation of plasmid DNA from E. coli cells.
3. Digestion of plasmid DNA with restriction enzymes.
4. Amplification of a DNA fragment by PCR.
5. Complementation of β−galactosidase for Blue and White selection.
2.3 References
1. Brown, T.A. (2010) Gene Cloning and DNA Analysis (6th ed.), Wiley-Blackwell
publishing (Oxford, UK), ISBN: 978-1-4051-8173-0.
2. Glick B.R., Pasternak, J.J. and Patten, C.L., (2010) Molecular Biotechnology:
Principles and Applications of Recombinant DNA (4th ed.), ASM Press (Washington
DC), ISBN: 978-1-55581-498-4 (HC).
3. Michael R Green and J. Sambrook (2014) Molecular Cloning: A laboratory manual,
(4th ed.), Cold spring Harbor laboratory press (3vol.), ISBN: 978-1-936113-42-2
4. Primrose, S.B., and Twyman, (2006) Principles of Gene Manipulation and Genomics
(7th ed.), R. M., Blackwell publishing (Oxford, UK) ISBN:13: 978-1-4051-3544-3.
67

I. Students will learn Describe different systems, and The students will be given
about the their applications with case home assignment at the end
significance of studies using Chalk and board of first unit.
Restriction and along with power point
Modification presentations.
System, properties
and uses of different
restriction and
modification
enzymes and
DNA as well as
Methods to ligate
DNA molecules
II. Students will learn Students will be asked to orally The students will undergo
about the biology of revise the previous class before internal test with syllabus
different types every new class helping them in covered in the two units
of vectors systems better understanding and their and their answers will be
including doubts cleared, if any. discussed in the following
plasmids and class.
bacteriophages used
in prokaryotes and
eukaryotes along
with their
applications.
III. Students will know Chalk and board along with The students will be given
about DNA transfer power point presentations, home assignment at the end
to cells, regular question answer of third unit.
distinguishing activities. Consultation of text
between books.
recombinants and
non-recombinants
and to identify a
specific clone among
many clones in a
library
IV Students will earn Concepts will be taught using The students will undergo
about the signals that chalk and board and notes; internal test with syllabus
promote expression Power point presentations for covered in the third and the
of heterologous images for clarity of concepts; fourth units and their
proteins from answers will be discussed
expression vectors in the following class.
and their purification
from the medium
68
V. Students shall Teaching using chalk and The students will be given
become aware of the board; Oral discussion sessions home assignment at the end
basic process of in the class. of fifth unit.
PCR, different types
of PCR and DNA
sequencing
techniques
VI. The students shall be Teaching and learning activity The students will undergo
able to understand will mainly include extensive internal test with syllabus
how theoretical discussions; chalk and board covered in the fifth and the
knowledge of RDT teaching; Discussion about sixth units and their
translates into principle and logic behind each answers will be discussed
production of methods and experiment. in the following class.
commercially useful
proteins that are used
in medicine and
about creating
GMOs, while
maintaining strong
ethics
4. Key Words:
Genetic Engineering, Recombinant Proteins expression and purification,

Biotechnology, cloning
69
CORE PAPER
Immunology (BCH C-14)
Semester VI
1. Course Objective
This course describes the molecular and cellular basis of the development and function
of the immune system. The course will provide the basic framework in immunology that will
cover the major topics including innate and adaptive immunity, antibodies and antigens, the
molecular events leading to the generation of antibody, humoral and cell mediated adaptive
immune response, hypersensitivity, self-tolerance, autoimmunity and vaccines.
Upon completion of this course, a student will be able to:
 Trace the history and developments in immunology.

 Have an overview of the immune system including cells, organs and receptors.
 Describe the basic mechanism, differences and functional interplay of innate and
adaptive immunity
 Understand Antigens & its Recognition, antigen processing and presentation
 Understand the structure & functions of different classes of Immunoglobulins,
and understand the genetic basis of antibody diversity
 Define the cellular and molecular pathways of humoral and cell-mediated immune
responses
 Describe the mechanisms involved in different types of hypersensitivity
 Explain the principles of tolerance and autoimmunity
 Understand Immunotherapies and basic concept of Vaccines
 Summarize role of immunity in protection against pathogens
2.2 Course contents
THEORY
UNIT I: Immune System and Innate Immunity No. of hours: 10
Historical Perspective, Innate and Adaptive Immunity, Hematopoiesis, cells of the immune
system, primary and secondary lymphoid organs and tissues. Anatomical barriers, cell types of
innate immunity, soluble molecules and membrane associated receptors (PRR), connections
between innate and adaptive immunity, localized and systemic response. Complement
activation by classical, alternate and MB lectin pathway, biological consequences of
complement activation, regulation and complement deficiencies
70
UNIT II: Antigens and Antibody No. of hours: 12
Antigens, carriers, adjuvants and haptens, factors responsible for immunogenicity, B and T cell
epitopes. Structure, classes and subclasses of immunoglobulins (Ig, Ig fold), effector functions
of antibody, antigenic determinants on Ig, Ig super family. Monoclonal antibodies production
and applications
UNIT III: Biology of the B Lymphocyte & Humoral Immunity No. of hours: 10
Dreyer-Bennett hypothesis, multigene organization of Ig locus, mechanism of V region DNA

rearrangement, mechanisms of antibody diversity. Antigen independent phase of B cell
maturation and selection, humoral response – T-dependent and T-independent response,
anatomical distribution of B cell populations
UNIT IV: Biology of the T Lymphocyte & Cell Mediated Immunity No. of hours: 12
General organization and inheritance of MHC, structure, distribution and role of MHC class I
and class II proteins, pathways of antigen processing and presentation. Structure and role of T
cell receptor (TCR) and co-receptor, T cell development, generation of receptor diversity,
selection and differentiation. General properties of effector T cells, cytotoxic T cells (Tc),
natural killer cells; NK - T cells and antibody dependent cellular cytotoxicity (ADCC).
UNIT V: Autoimmunity and Hypersensitivity No. of hours: 10
Self-tolerance and possible mechanisms of induction of autoimmunity, Organ specific and

systemic autoimmune diseases, Gell and Coombs classification, IgE mediated (Type I)
hypersensitivity, antibody mediated cytotoxic (Type II) hypersensitivity, immune complex
mediated (type III) hypersensitivity and delayed type (Type IV) hypersensitivity
UNIT VI: Transplantation Immunology and Vaccines No. of hours: 6
Immunological basis of graft rejection, clinical manifestations, immunosuppressive therapy

and privileged sites. Vaccines - active and passive immunization, types of vaccines
PRACTICALS
1. Isolation of lymphocytes from blood / spleen.

2. Purification of immunoglobulins from serum
3. Assays based on precipitation reactions - Ouchterlony double immunodiffusion (DID)
and Mancini radial immunodiffusion (SRID).
4. Assays based on agglutination reactions - Blood typing (active) & passive
agglutination.
5. Enzyme linked immunosorbent assay (ELISA) & DOT ELISA
71
2.3 References
1. Coico, R and Sunshine, G. (2009) Immunology: A Short Course (6th ed.), John Wiley&
sons, Inc (New Jersey), ISBN: 978-0-470-08158-7.
2. Kindt, T.L., Goldsby, R.A. and Osborne, B.A. (2007) Kuby Immunology (6th ed.), W.H
Freeman and Company (New York), ISBN:13: 978-0-7167-8590-3 / ISBN: 10:0-7617-
8590- 0.
3. Murphy, K., Mowat, A., and Weaver, C.T. (2012) Janeway’s Immunobiology (8th ed.),
Garland Science (London & New York), ISBN: 978-0-8153-4243-4

I. Students will be Chalk and board method will Students will be asked to
taught about the be used and powerpoint correlate the importance of
historical perspective presentation for depicting the immunity and health by
of immunology, structure of cells and asking them to site
They will learn about hematopoiesis examples from their
the cells and organs experience
of the immune
system and innate
immune
mechanisms..
II. Students will be Chalk and board method will MCQ based assignments
explained the be used and powerpoint will be given to students to
concept of foreign presentation for depicting the check their understanding
molecules acting as structure of antibodies of the subject. Students
antigens. What are will be asked to come up
antibodies and their with examples where
basic structure will antigen – antibody
be dealt with. Will interactions can be utilized
focus on how antigen for diagnostic purposes.
and antibody can This will help them to
interact with each understand the importance
other of these components of the
immune system.
III. Students will Chalk and board method will Discussion related to
understand how be used and powerpoint transcription and
antibodies are presentation for understanding translation of proteins will
generated in the antibody diversity and be held and comparisons
body. They will production with antibody production
understand the will be highlighted. Class
importance of tests will be taken.
humoral response in
infections
72
IV Students will be Chalk and board method will Students will be asked to
exposed to the be used and powerpoint focus on the functioning of
cellular arm of presentation for understanding T cell as opposed to B
immunity. The The interaction between cells. Certain articles
various cells which various cells related to these basic
participate in cellular concepts will be discussed
response will be in groups
dealt with. Cytotoxic
action of T cells will
be discussed
V. Students will Chalk and board method will Interaction with students
understand the be used and supplemented with will be held in form of
importance of powerpoint presentation. some case studies .Quiz
regulated immune will be held.
response. What will
happen if the
immune response is
exaggerated will be
explained with
examples. The
concept of
autoimmunity will
also be explained
VI. Importance of Chalk and board method will Students will be asked to
immunity will be be used and supplemented with read articles related to
highlighted by powerpoint presentation. immunity and its
explaining the intervention in medicine
importance of and group presentation on
vaccines and these topics will be
transplantation of encouraged.
organs.
4. Keywords
Immunity, Innate Immunity, Adaptive Immunity, Antigens, Antibodies, Antibody

Diversity, Antigen Processing & Presentation, MHC, Humoral Response, Cell mediated
Immunity, Hypersenstivity, Tolerance, Autoimmunity, Vaccines
73
DISCIPLINE SPECIFIC ELECTIVE (DSE) COURSES
74
Nutritional Biochemistry (BCH DSE-1)
Semester - V
1. Course Objective
This course provides students with knowledge and understanding of the characteristics,
function, assimilation, distribution and deficiency of macro and micronutrients in the human
body. It involves integrated learning between the areas of Biochemistry and Nutrition.
At the end of the course, the students are expected to:
 Critically analyze and evaluate concepts in nutritional biochemistry that are important
for an understanding of human nutrition.
 Appreciate the biochemical underpinning of human nutrition in maintaining health.
 Demonstrate understanding of the biochemical basis of essentiality of macro and
micronutrients and their nutritional deficiencies.
 Be aware of techniques used in the assessment of nutritional status and nutritional
disorders.
 Understand drug nutrient interactions.
2.2 Course Contents
THEORY
UNIT I: Introduction to Nutrition and Energy Metabolism No. of hours: 6
Defining nutrition, role of nutrients. Unit of energy, biological oxidation of foodstuff.

Physiological energy value of foods, SDA. Measurement of energy expenditure, BMR and
RMR- factors affecting BMR. Recommended Nutrient Intakes (RNI) and Recommended
Dietary Allowances for different age groups.
UNIT II: Macronutrients No. of hours : 20
Food sources of carbohydrates, Review functions of carbohydrates. Factors

affecting Digestion, absorption and utilization. Glycemic index and glycemic load. Dietary
fiber and role of fibre in health. Role of Gut microbiome in maintaining health. Role of pre and
probiotics in nutritive health. Essential Fatty Acids; Functions of EFA, RDA, – excess and
deficiency of EFA. Dietary implications of fats and oils, Combination ratios of n6 and n3,
MUFA, PUFA and SFA Factors affecting Digestion, absorption and utilization. Importance
of the following: a) Omega – fatty acids. Omega 3/ omega 6 ratio b) Phospholipids c)
Cholesterol in the body d) Mono, Polyunsaturated and Saturated Fatty Acids. Review of
functions of proteins in the body, Digestion and absorption. Essential and Nonessential amino
75
acids. Complete protein, Amino Acid Availability, Antagonism, Toxicity, Imbalance, Amino
acid complementation and Supplementation in foods. Effects of deficiency. Food source and
Recommended Dietary Allowances for different age group. Amino acid pool. NPU,
Biological Value, Nitrogen balance. PEM:Marasmus and Kwashiorkor.
UNIT III: Micronutrients: Vitamins No. of hours : 12
Vitamin A, D, E, K and dietary sources, RDA, Adsorption, Distribution, Metabolism and

excretion (ADME), Deficiency. Role of Vitamin A as an antioxidant, in Visual cycle,
dermatology and immunity. Role of Vitamin K in Gamma carboxylation. Role of Vitamin E
as an antioxidant. Extra-skeletal role of Vitamin D and its effect on bone physiology.
Hypervitaminosis. Vitamin C- Dietary sources, RDA, Adsorption, Distribution, Metabolism
and excretion (ADME); role as cofactor in amino acid modifications. The B Complex vitamins-
Dietary sources, RDA, Adsorption, Distribution, Metabolism and excretion (ADME);
Thiamine -TPP role in metabolism and deficiency disease; Niacin- Metabolic interrelation
between tryptophan, Niacin and NAD/ NADP; Vitamin B6-conversion to Pyridoxal
Phosphate. Role in metabolism, Biochemical basis for deficiency symptoms; Vitamin B12 and
folate - metabolic role, homocysteine cycle, Biochemical basis for deficiency symptoms.
UNIT IV: Micro Minerals and trace elements No. of hours : 10
Calcium, Iron and Phosphorus- Distribution in the body digestion, Absorption, Utilization ,
Transport, Excretion, Balance, Deficiency, Toxicity, Sources, RDA. Iodine, Fluoride, Mg,
Cu, Zn, Se, Manganese, Chromium, Molybdenum Distribution in the human body, Physiology,
Function, deficiency, Toxicity and Sources
UNIT V: Assessment of Nutritional status No. of hours : 6
Direct methods of assessment-Anthropometric measurements; Biochemical assessment;

clinical signs; dietary records and nutrient intake. ROS assessment, GTT and glycosylated Hb,
Differential diagnosis of B12 and folate.
UNIT VI: Food-drug interactions and Nutraceuticals No. of hours : 6
Nutrient interactions affecting ADME of drugs. Drug induced nutrient deficiency: Alcohol,
Antibiotics, Anti-malarial drugs. Food as medicine: turmeric, garlic, ginger, cumin, asafoetida
PRACTICALS
1. Anthropometric identifications for nutrition related diseases

2. Blood Lipid profile
3. Determination of oxidative stress: TBARS in serum, antioxidant enzymes in
hemolysate/plant sources.
4. Estimation of vitamin in drugs/food/serum.
5. Estimation of minerals in drugs/food/serum.
6. Estimation of glycosylated haemoglobin
7. Determination of nutritive value of foods
8. Case studies on nutritional disorders.
76
2.3 References
1. Coombs Jr. G. F., (2008). The vitamins, Fundamental aspects in Nutrition and Health.
Elsevier’s Publications. ISBN-13- 978-0-12- 183493-7.
2. Devlin, T. M., (2011). Textbook of Biochemistry with Clinical Correlations. John Wiley
& Sons, Inc. (New York), ISBN: 978-0-4710-28173-4.
3. Mahan, L.K., Strings, S. E., Raymond, J. (2012) Krause’s Food and Nutrition Care
process. Elsevier’s Publications. ISBN: 978-1-4377-2233-8.
4. Rosalind Gibson (2005). Principles of Nutritional Assessment. Oxford University
Press. ISBN: 9780195171693
5. Tom Brody (1999). Nutritional Biochemistry (2nd ed). Harcourt Braces.
ISBN:9814033251, 9789814033251.

No. Activity
I. Basic concepts of nutritional Chalk and board teaching Assessment through
biochemistry that are for basic concepts regular discussion,
important for an Quiz and solving
understanding of human numerical problems
nutrition will be learnt. on energy
expenditure
II. Understand the biochemical Power point presentations Regular oral
basis and nutritional will be used to teach about question answer
importance of macronutrients. essential macronutrients. sessions in class,
They will learn the importance Discussions will be held to case study
of gut biome in maintenance clarify the concepts. evaluations and
of health and the role of Internal assessment
dietary fiber in maintaining a test
good gut microbiome and will
understand the concepts of
diet composition in governing
nutrient assimilation
III. Development of understanding Chalk and board teaching, Oral question-
of the ADME and essentiality power point presentation on answer sessions in
of fat and water soluble essential vitamins and their class, assessment
vitamins. They will also learn deficiency disorders, through test/quiz
the biochemical mechanisms historical perspective on and case study
for the symptoms of vitamin nutritional deficiencies analysis.
deficiencies and excesses Practical diagnosis of any
one vitamin deficiency.
IV Appreciate the importance of Black board teaching of the Test and assignment
mineral macronutrients with basic concepts and Case study analysis.
special emphasis on calcium powerpoint presentations Power point
and iron on regulation of presentations
micromineral homeostasis on chemistry of
Practical diagnosis of any vitamins.
one mineral deficiency.
77
V Get acquainted with the Chalk and board teaching Assessment test and
techniques used in the and discussion on case case study
assessment of nutritional studies bases on evaluation
status and nutritional anthropometry and
disorders. biochemical estimations
Anthropometric
assessment-
Practical class.
Practical assessment of
oxidative stress.
VI. Gain knowledge about drug Power point presentation Test/quiz on various
nutrient interactions. and chalk and board groups of drugs and
teaching. their effect on
nutrient availability
Power point
presentations
Onnutraceuticals.
4. Keywords
Nutrition, macro nutrients, micro nutrients, nutrient assessment, nutrient deficiency
78
Advanced Cell Biology (BCH DSE-2)
Semester - V
1. Course Objective
The course aims to provide advanced knowledge of the function of cellular organelles,
the structure and function of cytoskeleton and its role in motility. The course will also provide
details of cellular interaction with cells and tissues around and the molecular regulation of cell
growth and cell death. The course will outline the molecular details of the origin of cancer and
the diagnosis and treatment.
The learning outcomes will be as follows:
 Students will develop understanding of the principle and application of some of the
classical and advanced cell biology techniques
 Students will be able to describe the role of organelles in the secretion of mature
proteins and key role of the cytoskeleton in the living cell.
 Students will be able to understand the factors regulating mitosis, meiosis, apoptosis
and necrosis. They will also be able to comprehend the role and therapeutic value of
stem cells.
 Students will be able to understand the genetic basis of development of cancer, the
molecular diagnosis and molecular drugs which are used for chemotherapy.
2.2 Course Contents
THEORY
UNIT I: Advanced Methods in Cell Biology No. of hours: 6
Principle and application of ultracentrifugation
UNIT II: Protein Sorting and Secretory Pathway No. of hours: 16
Transport of proteins across nuclear envelope; Regulation of nuclear protein import and export.
Overview of the endomembrane system; Targeting, modification and sorting of proteins from
and into Endoplasmic Reticulum; Synthesis and targeting Mitochondrial protein; Chloroplast
Proteins and Peroxisomal proteins; Mechanism of Vesicular Transport; Coat Proteins and
Vesicle Budding; Vesicle Fusion; Targeting of Proteins
79
UNIT III: Cytoskeleton and Cell Motility No. of hours: 10
Function and origin of the cytoskeleton; Organization and assembly of Actin Filaments and
Myosin; Assembly and organization of Microtubules and Intermediate Filaments; Motor
proteins of microtubules and their functions. Cell movement.
UNIT IV: Cell Division and its Regulation No. of hours: 10
Overview of the cell cycle; Eukaryotic cell cycle; Events of Mitotic Phase; Cytokinesis; Events
of Meiosis And Fertilization; Regulation of Cell Division and Cell Growth;
UNIT V: Cell Death and its Regulation No. of hours: 8
Apoptosis and Necrosis, Application of stem cells in health and disease. Hematopoiesis,
Embryonic Stem Cells and Therapeutic Cloning.
UNIT VI: Molecular Basis of Cancer Biology No. of hours: 10
Development and causes of cancer; Genetic basis of cancer; Oncogenes, Tumor Viruses;
Molecular approach to cancer treatment.
PRACTICALS
1. Techniques of Plant /Animal Tissue Culture

2. Study of pinocytosis by paramecium under microscopy
3. Calculating viability of bacterial cells after exposure of the bacterial culture to UV rays
4. Preparing temporary mount of nerve cell from mammalian spinal cord
5. Differential centrifugation of cell and validation of separated organelles by enzyme
markers
6. Study of cell- cell agglutination by lectin and calculation of haem-agglutination titre.
7. Demonstration of phagocytosis/apoptosis
2.3 References
1. Cooper, G.M. and Hausman, R.E., (2009). The Cell: A Molecular Approach.(7th ed.).
ASM Press & Sunderland (Washington DC), Sinauer Associates, MA. ISBN:978-0-
87893-30.
2. Karp, G., (2010). Cell and Molecular Biology: Concepts and Experiments (8th ed.).
John Wiley & Sons. Inc. ISBN : 978-1-118-65322-7.
3. Kleinsmith, L. J., Hardin, H., Wayne G., Becker, M. (2009). The World of the cell (7th
ed.). ISBN-13: 978-0805393934 / ISBN-10: 0805393935.
1. Alberts, B., Johnson, A., Lewis, J., and Enlarge, M. (2008). Molecular Biology of the
Cell. (5th ed.). Garland Science (Princeton), ISBN:0-8153-1619-4 / ISBN:0-8153-1620-
8.
80
2. Lodish, H., Berk, A., Zipursky, S.L., Matsudaira, P., Baltimore, D. and Darnell. J.,
(2012). Molecular Cell Biology (7th ed.). W.H. Freeman & Company (New York).
ISBN:13:978-14641-0981-2 / ISBN:10: 1-4641-0981-8.

I. The students will be Basic concepts will be Internal assessment tests
given an in-depth explained with the help of and quiz will be
understanding of the power point presentations conducted. Students will
principles, working, /chalk board teaching along be assigned various topics
application and with informative audio-visuals. and will be asked to
limitations of various The students will be taken to deliver a power point
advanced techniques prestigious institutes during presentation on the
used in cell biology educational trips to further assigned topics.
help them grasp the concepts
taught to them in class.
II. The students will The students will learn to The students will be
gain knowledge correlate the advanced assessed by assignments
regarding the roles techniques learnt by them in and internal tests.
various organelles in the previous unit with the
protein sorting in the organelles learnt in this unit They will be required to
cell. They will also with the help of electron identify the various
learn about the micrograph diagrams of the pathways adopted by the
mechanisms various organelles of the cell. proteins for proper folding
involved in vesicular They will be given an insight and reaching correct
transport and cell- into the original experiments destination. They will also
cell/cell-virus fusion. conducted by scientists to be tested on their
discover the protein sorting understanding of
and secretory pathways of the difference between the
cell. The students will be various types of vesicular
taught using power point transport as well as steps
presentations and chalk board involved in fusion of
teaching. cells/cell-virus.
III. The students will The students will be taught the The students will be
learn about the basic concepts regarding the assessed by assignments
organization and various components of the and internal tests. Tests in
assembly of the cytoskeleton and their role in the form of quiz will be
components of the cell motility by using power held and students will
cytoskeleton like the point presentations and chalk mention the characteristics
actin and myosin board teaching. of each of the components
filaments; the of the cytoskeleton. They
microtubules and will also be quizzed about
intermediate as well their knowledge on the
as the cilia and types of cellular junctions,
flagella. They will method of polarization of
also learn about the cell etc.
81
various mechanism
of action of the
factors contributing
to cell motility.
IV The students will Basic concepts will be The students will be tested
learn the salient explained with the help of by asking them to prepare
features and phases power point presentations slides identify specific
of cell cycle. They /chalk board teaching along stages of cell division
will understand the with informative audio-visuals. observed by them, and its
various events that The students will observe the significance in cell
lead to the various stages of cell division division. The students will
progression of cell under the microscope, using also be assessed with
division – both various samples. assignments and internal
mitosis and meiosis. tests.
They will also
understand basic
differences between
the two types of cell
division, and the cell
types associated with
these divisions.
V. Students will learn Basic concepts will be Group discussions will be
the basic concept of explained with the help of conducted to elucidate the
cell death and the power point presentations importance of stem cells in
importance of /chalk board teaching along therapeutics. The students
programmed cell with informative audio-visuals. will also be assessed with
death. They will also assignments and internal
understand the tests.
various types and
importance of stem
cells along with their
application in
therapeutic cloning.
VI. The students will Basic concepts will be Internal assessment tests
learn the basic explained with the help of and quiz will be
concepts of cancer power point presentations conducted. Students will
biology and /chalk board teaching along be given assignments
understand how and with informative audio-visuals. outlining the various
why cancer develops sources of carcinogens in
in a system. They our surroundings. The
will also learn about assignment will also
the currently used require them to enlist the
approaches towards various food items that are
cancer treatment. popularly said help prevent
cancer and mention
scientific evidence if any,
to support these claims.
82
4. Keywords
Ultracentrifugation, FACS, FRET, Confocal Microscopy, Electron microscopy, Plant

tissue culture, Animal tissue culture, Immunihistochemistry, Cell-Cell
fusion, Posttranslational modification of proteins, secretory pathway, endocytosis,
phagocytosis, autophagy, Cytoskeleton, Cilia, Flagella, Cell-Cell interaction, Cell matrix
interaction, extracellular matrix, mitosis, meiosis, MPF, Apoptosis, Necrosis, Stem cell
application, Cancer, Oncogenes, Tumor virus, cancer treatment
83
Microbiology (BCH DSE-3)
Semester - V
The objective of the course is to trace the history of development of the discipline of
Microbiology and to emphasize the existence of the immense diversity in the microbial world
and maintenance of microbes under laboratory conditions. The course also aims to make the
students aware of both pathogenic as well as beneficial microbes to prepare students for higher
education in microbiology-related disciplines.
On successful completion of this paper, students should be able to:
 Identify different microbes

 Perform routine microbiological practices including sterilization, media preparation,
maintenance of microbial culture, staining etc.
 Carry out research using microbes.
 Test microbial culture for antibiotic resistance.
2.2 Course Contents
THEORY
UNIT I: History of Microbiology No. of hours: 8
History of development of microbiology as a discipline, Spontaneous generation versus

biogenesis, contributions of Anton von Leeuwenhoek, Joseph Lister, Paul Ehrlich, Richard
Petri, Charles Chamberland, Edward Jenner, Louis Pasteur, Robert Koch, Martinus W.
Beijerinck, Sergei Winogradsky, Alexander Fleming, Elie Metchnikoff and Emil von Behring
UNIT II: Diversity of Microbial world and Microbial Cell organization No. of hours: 14
Difference between prokaryotic and eukaryotic microorganisms. General characteristics of

different groups: Acellular microorganisms (Viruses, Viroids, Prions) and Cellular
microorganisms (Bacteria, Archaea, Algae, Fungi and Protozoa) with emphasis on distribution,
occurrence and morphology. Cell-wall: Composition and detailed structure of Gram positive
and Gram negative cell walls, mechanism of Gram’s staining. Cell Membrane: Structure,
function and chemical composition of bacterial and archaeal cell membranes.
84
UNIT III: Microbial Nutrition and Growth No. of hours: 14
Nutritional types of microorganisms, growth factors, culture media- synthetic and complex,
types of media; isolation of pure cultures, growth curves, mean growth rate constant, generation
time; influence of environmental factors on growth of microbes: effect of pH, temperature,
solute, oxygen concentration, pressure and radiations. Sterilization, disinfection and
antiseptics. Use of physical methods (heat, low temperature, filtration, radiation) and chemical
agents (phenolics, halogens, heavy metals, sterilizing gases) in microbial control.
UNIT IV: Pathogenicity of Microorganisms and Antimicrobial Chemotherapy

No. of hours: 8
Introduction to pathogenic microbes; Bacteria, Viruses, Algae, protozoa and fungi. General
Characteristics of antimicrobial drugs, determining the level of microbial activity: dilution
susceptibility test and disc diffusion test. Range of activity and mechanism of action of
penicillin, vancomycin and tetracycline.
UNIT V: Food and Industrial Microbiology No. of hours: 16
Importance of microbiology in food and industries; Basic design of fermenter, continuous and
discontinuous culture. Preparation of fermented food products such as yoghurt, curd and
cheese. Preparation of alcoholic beverages like wine and beer. Single cell proteins. Treatment
of waste water (Municipal treatment plant) and sewage. Bioremediation and biodegradation.
PRACTICALS
1. To prepare and sterilize the culture media for the growth of microorganisms
2. To perform various culture transfer techniques: Solid to solid (streaking), liquid to solid
(spreading), liquid to liquid, solid to liquid and determine CFU/ml
3. To stain bacteria using methylene blue.
4. To perform gram staining
5. To prepare temporary mount of algae (spirogyra)
6. To prepare temporary mount of fungi (Penicillium)
7. Study of different shapes of bacteria, fungi, algae, protozoa using permanent
slides/pictographs
2.3 References
1. Chan, M. J., Krieg E. C. S., Pelczar, N. R. (2004) Microbiology (5th ed.). McGraw
Hill International. ISBN 13: 9780094623206.
2. Willey, J., Sherwood, L., Woolverton, C. (2017). Prescott's Microbiology (10th ed.).
McGraw Hill international. ISBN 13: 9781259657573.
1. Cappuccino J. G., and Sherman N., Microbiology: A Laboratory manual (10th ed.).
Benajamin/ Cummings. ISBN 13: 9780321840226.
85
2. Madigan, M. T., Martinko J. M., & Stahl D. A., (2010) Brock Biology of
Microorganisms (13th ed.). Pearson Education International. ISBN 13:
9780321649638.

I. Students will be able Power point presentations and Class test will be taken.
to understand the blackboard teaching. General Questions related to the
historical discussion with students about topic will be given in the
development and the topic taught to understand form of assignment
contributions of their knowledge.
various scientists in
the field of
microbiology
II. Students will be able Power point presentations and Class test will be taken at
to understand the blackboard teaching. Hands on the end of module.
existence and experience on gram staining Questions related to the
diversity of the technique during practical topic will be given in the
microbial world. classes form of assignment.
They will get Students will also be
familiarize with the assessed based on their
Gram staining ability to prepare gram-
techniques stained slides.
III. Students will learn Blackboard teaching. principle Students will be assessed
about the nutritional and working of some of the by asking oral questions
requirements of instruments will be explained and also assessed during
microorganisms. using online resources. practical classes for the
They will also learn Experience on handling preparation of media and
about the various various instruments during handling of instruments
physical and practical classes
chemical methods
used for the control
of microbial growth.
IV Students will gain Blackboard teaching. General Class test will be taken at
knowledge about discussion with students about the end of module.
pathogenic microbes the existence of disease Assignment will be given
and characteristic causing microbes in our day- to understand the concept
features of today life. of mechanism of action of
antimicrobial drugs. different antimicrobial
drugs.
V. Students will be able Blackboard teaching. Students will be evaluated

to understand the Powerpoint presentation and on the basis of
86
industrial oral discussions in the class presentations and
applications of assignments
microbes
4. Keywords
Microorganisms, diversity, culture, Pathogenicity, industrial applications
87
Molecular Basis of Infectious Disease (BCH DSE-4)
Semester - VI
1. Course Objective
The course aims to provide knowledge about various microbial infectious agents that
cause diseases in humans, the concepts of treatment and the biochemical basis of mechanism
of action and drug resistance for various antimicrobial agents. The course will also provide
outline of the various strategies that are employed for preventing infectious diseases and the
role of vaccination in eradication of diseases. It will cover the concept of emergence and re-
emergence of diseases and idea of bio-terrorism and its impact worldwide. The course will also
summarize the significance of hygiene, sanitation, drugs and vaccination in prevention and
eradication of infectious diseases.
Upon completion of this course, a student will:
 Understand various classes of pathogens and their mode of action and transmission.
 Be exposed to the molecular basis of treatment, diagnosis and vaccine design strategies
for all the diseases listed.
 Gain insight into host immune responses that ensue subsequent to infection.
 Learn the details of diseases such as tuberculosis, AIDS and malaria which are highly
prevalent in Indian subcontinent.
THEORY
UNIT I: Infectious diseases: an introduction No. of hours : 7
Classification of infectious diseases, Nosocomial infections; Patterns of Disease; Measuring

infectious disease frequency; Past and present emerging and re-emerging infectious diseases
and pathogens. Source, reservoir and transmission of pathogens. Safety measure when
working with pathogen biosafety levels, infection and evasion
UNIT II: Strategies for management of infectious diseases No. of hours : 4
Role of drugs, vaccines, hygiene and sanitation in prevention, transmission control and
treatment of infectious diseases
UNIT III: Diseases caused by bacteria No. of hours : 20
Classification of bacterial pathogens based on structure and nutritional requirements; Overview

of bacterial virulence factors and host pathogen interactions; detailed study of tuberculosis:
History, causative agent, molecular basis of host specificity, infection and pathogenicity,
diagnostics, therapeutics and vaccines, drug resistance and implications on public health. Other
88
bacterial diseases - virulence factors, host pathogen interaction, symptoms, diagnosis, vaccines
and drugs against - Typhoid, Diphtheria, Pertussis, Tetanus, Botulism Cholera, Anthrax and
Pneumonia
UNIT IV: Diseases caused by viruses No. of hours : 15
Structure of viruses, Baltimore system for virus classification; Overview of viral virulence
factors and host pathogen interactions; detailed study of AIDS: history, causative agent,
pathogenesis, diagnostics, drugs; other viral diseases including hepatitis, Influenza (Antigenic
shift and antigenic drift), Rabies, Dengue and Polio; Chicken Pox, Herpes Virus
UNIT V: Diseases caused by parasites No. of hours: 8
Detailed study of Malaria: history, causative agents, vectors, life cycle, Host parasite
interactions, diagnostics, drugs, vaccine development. Other diseases including Leishmaniasis
and Amoebiasis, Giardiasis and Trypanosoma infections
UNIT VI: Diseases caused by fungi No. of hours: 6
Fungal diseases such as Candidiasis, Sporotrichosis, Aspergillosis and Ring worm: general
disease characteristics, medical importance, pathogenesis, diagnosis and treatment
PRACTICALS
1. Isolation and enumeration of bacteriophages (PFU) from water/sewage sample

2. WIDAL test as a diagnostic test for typhoid
3. To perform Gram staining of bacterial samples
4. Acid fast staining of non-pathogenic Mycobacterium
5. Permanent slides of pathogens: Mycobacterium tuberculosis, Leishmania, Plasmodium
falciparum
6. MIC determination using Kirby Bauer / Alamar Blue assay
7. To prepare temporary mount of fungi and identify through staining
8. Research and presentation on current trends in infectious diseases
2.3 References
1. Jawetz, Melnick & Adelbergs (27th ed.), Medical Microbiology. McGraw Hill
Education. ISBN-10: 0071790314; ISBN-13: 978-007179031.
2. Kenneth J. Ryan, C., George Ray (2010), Sherris Medical Microbiology: An
introduction to infectious diseases. McGraw-Hill. ISBN-13: 978-0071604024 ISBN-
10: 0071604022
3. Prescott, Harley, Wiley, J.M., Sherwood, L.M., Woolverton, C.J. Klien's (2008).
Microbiology (7th ed.). Mc Graw Hill International Edition (New York) ISBN: 978-
007-126727
89

I. Students will develop an Revision of concepts Group discussion and quiz
understanding of important covered in the previous will be conducted, and
terminologies used in class will be done. This students will be given
infectious diseases. They will be followed by assignments
will develop an traditional chalk and
understanding of board teaching aided
transmission of pathogens with Power Point
and will gain insight into presentations
host immune responses
that ensue following
infection.
They will understand the
importance of biosafety
equipment for people who
work on infectious disease
causing pathogens
II. Students will learn the Revision of concepts Class tests will be
strategies used for covered in the previous conducted, and students
management of infectious class will be done. This will be asked to deliver
diseases i.e. prevention, will be followed by Power Point presentations
transmission control and traditional chalk and on the assigned topics
treatment of infectious board teaching aided
diseases with Power Point
presentations
III. Students will learn Revision of concepts Group discussion, Quiz
classification of bacteria covered in the previous will be conducted, and
and study various bacterial class will be done. This students will be asked to
virulence factors. Students will be followed by deliver Power Point
will understand the traditional chalk and presentations on the
pathophysiology of the board teaching aided assigned topics
Mycobacterium and study with Power Point
ways to prevent and treat presentations
Tuberculosis. They will
also learn about various
bacterial diseases
(Typhoid, Diphtheria,
Pertussis, Tetanus
Botulism, Cholera,
Anthrax, Pneumonia) their
molecular mechanisms and
intervention strategies
IV Students will learn about Revision of concepts Group discussion, Class
Baltimore classification covered in the previous tests will be conducted,
system of viruses and viral class will be done. This and students will be given
90
virulence factors. will be followed by assignments and will be
They will understand the traditional chalk and asked to give PowerPoint
pathophysiology of the board teaching aided presentations on the
HIV, Influenza and with Power Point assigned topics
Hepatitis virus and study presentations
ways to prevent and treat
AIDS, Influenza and
Hepatitis. Students will
learn about other various
viral diseases (Chicken
Pox, Herpes, Rabies,
Dengue and Polio) their
molecular mechanisms,
diagnosis and intervention
strategies.
V. Students will learn about Revision of concepts Quiz, Class tests will be
various parasitic diseases, covered in the previous conducted, and students
host parasite interaction, class will be done. This will be asked to deliver
their molecular will be followed by Power Point presentations
mechanisms of infection, traditional chalk and on the assigned topics
diagnosis and intervention board teaching aided
strategies with Power Point
presentations
VI. Students will learn about Revision of concepts Class tests will be
various fungal diseases, covered in the previous conducted, and students
their molecular class will be done. This will be asked to deliver
mechanisms, diagnosis and will be followed by Power Point presentations
intervention strategies traditional chalk and on the assigned topics
board teaching aided
with Power Point
presentations
4. Keywords
Infection, Pathogen, Immune response, Diagnosis, Vaccines, Diseases
91
DISCIPLINE SPECIFIC ELECTIVE PAPER
Plant Biochemistry (BCH DSE-5)
Semester - VI
The course aims at providing deep understanding of metabolic processes in plants and
the role of different biosynthetic pathways in plant growth and development. The course will
also impart basic concepts and applications of plant tissue culture.
Successful completion of this course will provide students with the following learning
outcomes:
 Understanding of plant cell structure and organization.

 Concept of the biochemical processes and metabolic pathways specific to
plants, including photosynthesis, photorespiration, cell wall biosynthesis, nitrogen
fixation and assimilation and plant secondary metabolism.
 Insight on how plants have evolved to cope up with the different stress conditions.
 Knowledge of the basic concepts of plant tissue culture and its application in generating
transgenic crops.
2.2 Course Contents
THEORY
UNIT I: Introduction to plant cell structure and carbon fixation No. of hours: 16
Introduction to Plant cells, Plasma membrane, Vacuole and Tonoplast membrane, Cell wall,
Plastids and Peroxisomes. Photosynthesis and Carbon assimilation. Structure of PSI and PSII
complexes, Light reaction, Cyclic and non-cyclic photophosphorylation, Calvin cycle and
regulation; C4 cycle and Crassulacean acid metabolism (CAM), Photorespiration, Photo
inhibition of photosynthesis, Photosynthetic carbon reduction (PCR) cycle, Synthesis of
polysaccharides in plants.
UNIT II: Respiration No. of hours: 12
Overview of glycolysis, Alternative reactions of glycolysis, Regulation of plant glycolysis,

Translocation of metabolites across mitochondrial membrane, TCA cycle, electron transport
chain, Alternative NAD(P)H oxidative pathways; Cyanide resistant respiration.
92
UNIT III: Nitrogen metabolism No. of hours: 10
Biological nitrogen fixation by free living and in symbiotic association; Structure and function
of the enzyme nitrogenase. Nitrate assimilation: Nitrate and Nitrite reductase. Primary and
secondary ammonia assimilation in plants; ammonia assimilation by glutamine synthetase-
glutamine oxoglutarate amino transferase (GS-GOGAT) pathway. Seed storage proteins in
legumes and cereals.
UNIT IV: Regulation of plant growth and stress physiology No. of hours: 8
Introduction to plant hormones and their effect on plant growth and development, Regulation
of plant morphogenetic processes by light.Plant stress, Plant responses to abiotic and biotic
stresses, Water deficit and drought resistance, Flooding, Temperature stress, Salt stress, Ion
toxicity, Pollution stress and potential biotic stress (insects and diseases).
UNIT V: Secondary metabolites and toxins No. of hours: 8
Representative alkaloid group and their amino acid precursors, function of alkaloids. Examples
of major phenolic groups; simple phenylpropanoids, coumarins, benzoic acid derivatives,
flavonoids, tannins and lignin, biological role of plant phenolics, Classification of terpenoids
and representative examples from each class, biological functions of terpenoids.
UNIT VI: Plant tissue culture and biotechnology No. of hours: 6
Cell and tissue culture techniques, types of cultures: organ and explants culture, callus culture,
cell suspension culture and protoplast culture. Plant regeneration pathways: organogenesis and
somatic embryogenesis. Applications of cell and tissue culture and somoclonal variation.
Germplasm storage and cryo- preservation. Brief introduction to transgenic plants.
PRACTICALS
1. Induction of hydrolytic enzymes proteinases /amylases/lipase during germination

2. Extraction and assay of urease from Jack bean
3. Estimation of carotene/ascorbic acid/phenols/tannins in fruits and vegetables.
4. Separation of photosynthetic pigments by TLC.
5. Culture of plants (explants).
2.3 References
1. Buchann (2015). Biochemistry and Molecular Biology of plant. (2nd ed.). I K

International. ISBN-10: 8188237116, ISBN- 978047 07 14218
2. Caroline Bowsher, Martin steer, Alyson Tobin (2008). Plant Biochemistry. Garland
Science. ISBN 978-0-8153-4121-5.
3. Dey, P. M. and J.B. Harborne, J.B., (Editors) (1997). Plant Biochemistry.
Academic Press. ISBN-10:0122146743, ISBN-13:978-0122146749.
93
Additional Reading
1. Taiz, L. and Zeiger, E. (2010). Plant Physiology (5th ed.). Sinauer Associates Inc.
ISBN-13: 978-0878938667, ISBN-10: 0878938664.

I. Students will be introduced Teaching will be conducted .
to basic structure of plant through both black board Preparation of summary of
cell and roles of different mode and power point differences of plant cells
organelles. Students will presentation mode. Special from cells of various other
gain detailed knowledge on lecture will be organized on organisms; Retrieval of
the process of current aspects of original research papers on
photosynthesis. Students photosynthesis and carbon photosynthesis, carbon
will also learn about carbon fixation. assimilation, light
fixation by Calvin cycle (C3 reactions and associated
cycle), C4 cycle and topics. They will separate
Crassulacean acid photosynthetic pigments
metabolism (CAM). by TLC.
II. Students will gain insight Students will be asked to . Students will be given
into the process of orally revise the previous assignment on different
respiration in plants with class before every new class topics and will be asked to
major focus on how it is helping them in better deliver a power-point
different from animal understanding.. Teaching presentation on the
respiration. Further, the will be conducted through assigned topics.
students will understand the both black board mode and
importance of translocation power point presentation
of metabolites across mode.
mitochondrial membrane.
III. Students will learn in detail Classical black board and A written test will be
about how biological power point presentation conducted. Students will
nitrogen fixation is carried mode will be used for be assigned the task of
out by free living and teaching. Videos on the retrieving research papers
symbiotic bacterial topic will be used for where nitrogen
associations. Students will concept building metabolism in plants were
gain insight into nitrate and engineered. Debate as to
nitrite reductase and their whether nitrogen
role in nitrate assimilation. metabolism may be
This unit will also affected by changing
emphasize on ammonia environmental conditions.
assimilation by glutamine
synthetase-glutamine
oxoglutarate amino
transferase (GS-GOGAT)
pathway in plants.
IV Students will gain insight of Class room lectures, power
plant hormones and their point presentations,
94
effect on plant growth and MOOCs/ UGC e-pathshala/ The applications of stress
development. Students will Open education resources biology in the generation of
also understand how plants to be used. Stress biology is transgenic plants resistant
respond to various abiotic a significant research area to environmental stresses
and biotic stresses like in the University and to be reviewed. Interaction
water deficit and drought faculties will be invited for with University researchers
resistance, flooding, lectures. in the area.
temperature stress, salt
stress, ion toxicity,
pollution stress and
potential biotic stress
(insects and diseases).
V. Students will learn about Powerpoint presentations, . Students will be given
the significance of classroom lectures, videos assignment on topics
secondary metabolites and to be utilized. related to plant secondary
toxins in plants with the metabolites and their
help of examples of major biological role and
phenolic groups; simple applications. s They will
phenylpropanoids, review methods on the
coumarins, benzoic acid identification of such
derivatives, flavonoids, metabolites and estimate
tannins and lignin. It will some of them in laboratory
also help the students .
understand the biological
role of plant phenolics and
terpenoids.
VI. Students will gain Chalk and board teaching, Internal assessment test
knowledge about basic cell power point presentations, will be conducted. Students
and plant tissue culture videos on plant tissue will learn how to culture
techniques and their culture and biotechnology. explants in laboratories.
application in generation of Research papers will be They will identify
transgenic plants. This will discussed. transgenic plants in use and
help them learn the concept their status in India.
of organ and explant
culture, callus culture, cell
suspension culture and
protoplast culture. Concepts
related to plant regeneration
pathways: organogenesis
and somatic embryogenesis
will be imparted to the
students.
4. Keywords
Plant cell, photosynthesis, respiration, nitrogen fixation and assimilation, secondary

metabolism, stress biology, plant tissue culture.
95
DISCIPLINE SPECIFIC ELECTIVE PAPER
Advanced Methodologies (BCH DSE-6)
Semester - VI
The objective of the course is to provide students with a sound background of latest
techniques used in biochemistry research and to provide them with an understanding of the
principles underlying these techniques. The course is designed to impart laboratory skills in the
form of practical exercises so that students can apply this knowledge to augment their research
acumen and improve their understanding of the subject.
 Students will acquire knowledge about the principles and applications of latest methods
used to analyze nucleic acids and proteins.
 Students will learn about the principle and applications of microscopy and various cell
biology techniques.
 Students will also be exposed to various methods of labeling DNA, proteins and whole
cells and their applications in research.
 The course will also provide them an opportunity for hands-on-experience to develop
their laboratory skills expected of any biochemist working in a research lab.
2.2 Course Contents
THEORY
UNIT I: Methods for analysis of nucleic acids No. of hours :20
Hybridization methods: Southern blotting, Northern blotting, In situ hybridization, Colony

hybridization. Binding of nucleic acids with protein: DNA pull down assays, Electrophoretic
Mobility Shift Assay (EMSA), DNA footprinting, Primer Extension, Chromatin
immunoprecipitation (ChIP), ChIP on ChIP. Gene expression analysis: Reporter assays -
example luciferase assay, DNA Microarrays, RNA seq.
UNIT II: Methods for analysis of proteins No. of hours :20
Protein-Protein Interaction: Immunoprecipitation, Co-Immunoprecipitation (Co-IP), Pull

down assays, Yeast two hybrid, Protein fragment complementation assay, Western blotting,
Far western blotting, Protein microarrays, ELISA. Protein Separation: Isoelectric focusing, 2D
protein gel electrophoresis, 2D-DIGE, Pulse field Electrophoresis; Structural Analysis: Mass
Spectrometry, MS/MS, LC/MS.
96
UNIT III: Microscopy based methods No. of hours : 6
Fluorescence microscopy, Scanning electron microscopy, Transmission electron microscopy,

Confocal microscopy
UNIT IV: Cell Biology techniques No. of hours : 8
Cell culture and transfection, Immunohistochemistry, Immunofluorescence, Flow cytometry,

FACS, TUNEL assay, Non-invasive scanning of soft tissue
UNIT V: Labeling methods No. of hours : 6
Radioactive and Non-radioactive labeling: DNA, Proteins, Whole cells, Fluorescent labeling.
DNA, Proteins, bacteria, living cells; Metabolic labeling, Pulse chase analysis
PRACTICALS
1. Western Blotting
2. Southern hybridization
3. Labeling DNA with biotinylated primers using PCR
4. EMSA (virtual lab)
5. Protein Pull down assay
6. Virtual lab on Microarray profiling or 2D-DIGE
2.3 References
1. Ausubel, F.M. et al. (2012). Current protocols in molecular biology. New York: John
Wiley & Sons.
2. Bisen, P. S., & Sharma, A. (2013). Introduction to instrumentation in life sciences.
Boca Raton: CRC Press.
3. Bonifacino, J. S., Dasso, M., Lippincott-Schwartz, J., Hartford, J. B., & Yamada, K. M.
(Eds.). (1999). Current protocols in cell biology. New York: John Wiley.
4. Coligan, J. E., Dunn, B. M., Ploegh, H. L., Speicher, D. W., & Wingfield, P. T.
(1995). Current protocols in protein science. New York: John Wiley & Sons.
5. Coligan, J. E. et al. (1991). Current protocols in immunology. New York: John Wiley
& Sons.
6. Fu, H. (Ed.). (2004). Protein-protein interactions: Methods and protocols (Vol. 261).
Totowa, NJ: Humana.
7. Levine, S., & Johnstone, L. (2008). The ultimate guide to your microscope. New York:
Sterling Pub.
8. Schimmel. (2013). Biophysical Chemistry. MacMillan Higher Education.
9. Wilson, K., & Walker, J. (Eds.). (2010). Principles and techniques of biochemistry and
molecular biology (7th ed.). Cambridge: Cambridge Univ. Press.
97
1. Golemis, E., & Adams, P. D. (2005). Protein-protein interactions: A molecular cloning

manual (2nd ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
2. Green, M. R., & Sambrook, J. (2012). Molecular cloning: A laboratory manual (4th
ed., Vol. 1-3). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
3. Sheehan, D. (2010). Physical biochemistry: Principles and applications (2nd ed.).
Chichester: Wiley-Blackwell.

I. The student will Classroom teaching with Quizzes, assignments and
learn about the visual aids, power point analytical problem solving
methods used in presentations, videos, questions
analysis and discussions on applications
manipulation of
nucleic acid
II. The student will Classroom teaching with Assignments, class tests,
understand about the visual aids, power point analytical questions.
various techniques presentations, experimental Students will be asked to
involving protein- data from journals, discussions retrieve papers on protein-
protein interactions, protein interactions.
their separation, and
structural
characterization
III. The students will get Presentations, classroom Assignments, class tests,
familiar with teaching, audio and visual aids, class presentations, Mid-
microscopy based trip to a facility. MOOCs will term assessment
techniques and their be used.
application
IV The students will Powerpoint presentations, trip Assignments, class tests,
understand the basics to a facility to show class presentations
and application of instruments, audio& visual
various techniques in aids. Special lecture will be
the field of cell arranged by expert in cell
biology biology techniques.
V. The students will Classroom teaching, Assignments, class tests,
learn about the presentations, discussions to presentations on
different ways to learn how these methods are applications etc.
label cells, microbes, applied all the previous units Internal assessment tests
proteins and DNA will be conducted
4. Keywords
Southern Blotting, Colony hybridization, DNA footprinting, EMSA, Western Blotting,
Immunoprecipation, Pull down assay
98
GENERIC ELECTIVE (GE) COURSES
99
Biomolecules (BCH GE-1)
Semester - I
The objective of the course is to provide students with an understanding of

biomolecules, the basic building blocks that are vital for various life forms, focusing on their
key properties, biological roles and functions. The course also aims to outline organic and
physical aspects of biomolecules.
 Students will acquire knowledge about structure and function of proteins, RNA, DNA,
carbohydrates and co-enzymes
 The course will provide an understanding of how structure of biomolecules determine
their chemical properties
 Students will develop understanding of biochemistry at atomic level and appreciate
the biological importance of each biomolecule
2.2 Course Contents
THEORY
UNIT I: Biomolecules in their cellular environment No. of hours : 7
The cellular basis of life, structure and function of a cell and its subcellular components
(eukaryotes, prokaryotes); Physical properties and structure of water molecule, pH, Buffers,
biological buffer systems (body fluids and their principal buffers)
UNIT II: Amino Acid and Peptides No. of hours : 11
Introduction, general nature of amino acids, classification of amino acids, importance of amino
acids, modified and standard amino acids, physical and optical properties of aminoacids,
ionization of amino acids, buffering of amino acids, peptide bond, biologically important
peptides. Introduction to chromatography, separation of amino acid by paper chromatography
UNIT III: Carbohydrate Chemistry No. of hours : 11
Introduction; Definition, classification and functions of carbohydrates, monosaccharides,

disaccharides, polysaccharides, homo polysaccharides, hetero polysaccharides; Structure of
glucose, isomerism; keto aldo, D-and L- isomerism, optical isomerism, epimerism, anomerism,
Mutarotation, chemical properties of monosaccharides, action of strong acids, alkalis,
100
oxidation, reduction, osazone formation glycoside formation; Derivatives of
monosaccharides, phosphoric acid ester, amino sugar, deoxy sugar, sugar acids, sugar
alcohols, disaccharides maltose, lactose, sucrose. Homo polysaccharides - starch, glycogen,
cellulose, dextrin; Hetero polysaccharides - types of glycosoaminoglycans and functions of
glycoproteins
UNIT IV: Chemistry of Lipids No. of hours: 11
Introduction; Definition, classification and functions of lipids; Fatty acids; Essential fatty;
acids; Reactions of lipids; Triacylglycerol or neutral fat; phospholipids glycolipids; cholesterol;
Eicosaanoids; prosatglandins; lipoprotein
UNIT V: Chemistry of Nucleic Acid No. of hours : 11
Introduction, nucleic acid, nucleotide, biologically important nucleotides, synthetic analogues

of nucleotides or antimetabolites; DNA structure and function; Types of DNA; Organization
of DNA; RNA structure and function
UNIT VI: Vitamins and Coenzymes No. of hours : 8
Definition and classification of vitamins, water soluble vitamins, fat soluble vitamins,
occurrence and nutritional role. Coenzymes and their role in metabolism. Metal ion containing
biomoleculeus (heme, porphyrins and cyanocobalamine) and their biological role
PRACTICALS
1 Safety measures in laboratories.

2. Preparation of normal and molar solutions.
3. Preparation of buffers.
4. Determination of pKa of acetic acid and glycine.
5. Qualitative tests for carbohydrates, and nucleic acids.
6. Separation of amino acids/ sugars/ bases by thin layer chromatography
2.3 References
& Sons, Inc. (New York). ISBN: 978-0-4710-28173-4.
2. Nelson, D.L. and Cox, M.M. (2017). Lehninger: Principles of Biochemistry (7th ed.).
W.H. Freeman & Company (New York), ISBN:13: 9781464126116 / ISBN:10-
1464126119.
101

Unit No Course Learning Teaching & Learning Assessment Tasks
Outcomes Activity
I Student will learn the Chalk and board method Students will be
fundamental concepts of will be used and power asked to correlate
cellular basis of life, point presentation for the importance of
cellular structure of depicting the structure of these molecules
prokaryotes and cells and role of water in from their cells by
eukaryotes. They will also design of these molecules. take home
learn the role of water in assignments.
design of these molecules.
II Students will gain insight Chalk and board method MCQ based
into basic structures, will be used. Power point assignments will be
chemistry and property of presentation for given to students to
amino acids along with understanding these check their
derivatives of amino acids. structure and their role. understanding.
They will be introduced to
chromatography
III Understanding of the basic Chalk and board method MCQ based
chemistry, structure and and power point assignment will be
classification of all types presentation will be used given to students.
carbohydrates, along with for describing these Structures will be
their biological role. structures distribution shown for them to
&their biological role. identify the type
and class of
carbohydrate
IV Students will learn about Learning of individual Multiple choice
the basic building blocks students will be conducted questions, take
of lipids and the different by a traditional chalk and home assignments
categories of lipids in the board method and and regular Q&A
body with main emphasis supported by power point sessions during
being on understanding slides wherever class.
their structure. They will appropriate.
also be exposed to some
aspects of function of the
different lipids in the body
including their role as
cofactors, pigments and
signaling molecules.
V Students will learn the Regular question answer Students’
basic aspects of the sessions in the class to knowledge will be
structure of DNA and encourage student assessed via regular
RNA along with unusual participation. quizzes and take
structures of DNA. Regular chalk and board home assignments
Students will also be made teaching will be used.
aware of the other roles
that nucleotides can play
in the body.
102
VI Students will learn about Students will be Assessment of the
the nutritional roles of all communicated to mainly student learning
water soluble and lipid using chalk and board will be done by
soluble vitamins in the method with occasional home exams,
body along with their support taken from multiple choice
occurrence. They will also structures projected on quizzes and take
be made aware of how transparencies or power home assignments.
vitamins are crucial in point slides They will review
metabolism of the body. research papers as
well.
4. Keywords
Buffer, Amino Acids, Glucose, Disaccahrides, Polysaccharides, Lipids, Nucleic Acids,

Vitamins, Chromatography
103
Techniques in Biochemistry (BCH GE-2)
Semester – I / II
The objective of the course is to introduce various techniques to students that are used
in biological research as well as to provide them with an understanding of the underlying
principles of these techniques. The emphasis is also on experimental skills in the form of
practical exercises so that students can apply this knowledge to improve their understanding of
the subject for better execution of these techniques.
 Students will acquire knowledge about the principles and applications of

spectrophotometric and chromatography techniques used in a biochemistry lab.
 Students will learn about the principle and application of electrophoresis, centrifugation
techniques, cell culture and microscopic techniques.
 It will also give them an opportunity to get hands on experience to develop their
experimental skills expected from any biochemist working in a research lab.
2.2 Course Contents
THEORY
CREDITS: 4 TOTAL HOURS:60
UNIT I: Spectroscopic Techniques No. of hours: 15
Electromagnetic radiation, interaction of radiation with biomolecules, principle of UV-visible

absorption spectrophotometry, Lambert's Law, Beer's Law, working of a spectrophotometer.
Applications of UV-visible absorption spectrophotometry in biochemistry. Fluorescence
spectrophotometry: Phenomena of fluorescence, intrinsic and extrinsic fluorescence,
applications of fluorescence in biochemistry.
UNIT II: Chromatography No. of hours: 15
Preparation of sample, different methods of cell lysis, salting out, dialysis. Introduction to
chromatography. Different modes of chromatography: paper, thin layer and column.
Preparative and analytical applications. Principles and applications of: Paper Chromatography,
Thin Layer Chromatography, Ion Exchange Chromatography, Molecular Sieve
Chromatography, Affinity Chromatography.
UNIT III: Electrophoresis No. of hours: 12
Basic Principle of electrophoresis, Paper electrophoresis, Gel electrophoresis, discontinuous

gel electrophoresis, PAGE, SDS-PAGE, Native gels, denaturing gels, agarose gel
104
electrophoresis, buffer systems in electrophoresis, electrophoresis of proteins and nucleic
acids, protein and nucleic acid blotting, detection and identification (staining procedures),
molecular weight determination, isoelectric focusing of proteins.
UNIT IV: Centrifugation No. of hours: 8
Principle of centrifugation, basic rules of sedimentation, sedimentation coefficient. Various

types of centrifuges, low speed centrifuge, high speed centrifuge and ultracentrifuge, types of
rotors. Application of centrifugation, differential centrifugation, density gradient
centrifugation- zonal and isopycnic.
UNIT V: Microbiological/Cell culture techniques No. of hours: 5
Types of media, selective and enrichment media, sterilization methods, bacterial culturing,
CFU determination, growth curves, Generation/doubling times, cell counting, viable and non-
viable. Growth and maintenance of cultures, biosafety cabinets, CO2incubator. Staining
procedures, plating and microtony.
UNIT VI: Microscopy No. of hours: 5
Principle of light microscopy, phase contrast microscopy, fluorescence microscopy. Permanent

and temporary slide preparation, histology and staining.
PRACTICALS
1. Verification of Beer’s Law

2. Estimation of proteins by Biuret/Lowry method
3. Separation of amino acid acids by TLC/paper chromatography
4. To perform agarose gel electrophoresis
5. To isolate mitochondria by differential centrifugation
6. Visualization of cells by methylene blue
2.3 References
1. Boyer, R.F. (2012). Biochemistry Laboratory: Modern Theory and Techniques (6th ed.).
Boston, Mass: Prentice Hall. ISBN-13: 9780136043027.
2. Plummer, D. T. (1998). An Introduction to Practical Biochemistry. (3rd ed.). Tata
McGraw Hill Education Pvt. Ltd. (New Delhi). ISBN: 13: 9780070994874 / ISBN:10:
0070994870.
3. Wiley, J.M., Sherwood, L.M., Woolverton, C.J. (2017). Prescott’s Microbiology.
(10th ed.). McGraw Hill Higher Education. ISBN13: 9781259657573.
4. Wilson, K., Walker, J. (2010). Principles and Techniques of Biochemistry and
Molecular Biology, (7th ed.). Cambridge University Press. ISBN 9780521516358.
1. Cooper, T. G., (2011). The Tools of Biochemistry (2nd ed.). Wiley-Interscience

Publication (New Delhi). ISBN: 13:9788126530168.
105
2. Freifelder, D. (1982). Physical Biochemistry: Applications to Biochemistry and
Molecular Biology (2nd ed.). W.H. Freeman and Company (New York), ISBN:
0716713152 / ISBN:0716714442.

I Students will learn about Teaching using chalk and Problems will be
the principle and board; Oral discussion assigned related to
applications of sessions in the class. Beer’s Law and
spectrophotometry and Powerpoint presentations. Lambert’s Law to test
flourimetry. the understanding of
students.
II Students will learn the Previous classes will be Practical exercises are
principle of various revised. Group discussion designed whereby the
chromatographic sessions in the class. students get hands on
techniques like gel Powerpoint presentations. experience with these
filteration, Ion exchange. chromatography
techniques.
III Students will learn about Oral discussion sessions Various analytical
electrophoretic techniques, in the class. Chalk and problems will be
their principle and board teaching. assigned to students
applications in analyzing related to electrophoretic
proteins and nucleic acids separation.
IV Students will learn about Revision of the previous Demonstration with the
the basic rules of classes for a better help of centrifuges and
sedimentation, various understanding of the rotors to improve their
types of centrifuges and students. Demonstration understanding.
rotors. of various centrifuges.
Chalk and board teaching.
V Students will learn and Power point Various analytical
understand the different presentations; Teaching problems will be
cell culture and using chalk and board; assigned to students
microbiological techniques Oral discussion sessions related to cell counting.
used in biochemistry. in the class
VI Students will learn about Group discussion sessions Various analytical
various microscopes and will be held in the class problems will be
slide preparation, histology along with powerpoint assigned to students
and staining techniques. presentations related to working of
microscope.
4. Keywords
Spectrophotometry, Chromatography, Proteins, Nucleic Acids, Centrifugation and

Electrophoresis
106
Proteins and Enzymes (BCH GE-3)
Semester – II / III
The objective of this course is to provide overview of protein biochemistry and

enzymology to undergraduate students with diverse science backgrounds, since proteins and
enzymes are the most versatile functional entities in life with applications in various life
sciences research as well as in industry and biomedicine. The biochemical, structural,
functional and aspects of interaction of proteins and enzymes will be introduced in this course.
On successful completion of the course students will be:
 Familiar with unique features and characteristics of proteins and enzymes and their
applications in research, medicine and industry.
 Aware of the relationship between three-dimensional structure of proteins and enzymes
and their functions.
 Able to comprehend the basic mechanism of action of enzymes and their remarkable
regulation
 Aware of the principles of protein isolation, purification and characterization
 Able to gain hands-on-experience in handling proteins and enzymes from various
sources, thus improving their ability of learning and imbibing the basic concepts.
2.2 Course Contents
THEORY
UNIT I: Introduction to proteins and their structural organization No. of hours :10
Amino acids and their properties. Peptides and their biological significance - hormones,
antibiotics and growth factors. Diversity of proteins and their functions. Protein sequence -
Edman degradation. Solid phase peptide synthesis. Organization of protein structure - primary,
secondary, tertiary and quaternary structures. Conjugated proteins, multimeric proteins and
metalloproteins. Bonds in protein structures - covalent and non-covalent. Dihedral angles.
Ramachandran map, Secondary structure - helices, sheets and turns.
UNIT II: Three-dimensional structures and protein folding No. of hours: 12
Characteristics of tertiary and quaternary structures. Motifs and domains. Structure-function

relationship in proteins. 3D structures of myoglobin and hemoglobin. Oxygen binding curves,
influence of pH and effector molecules. Concerted and sequential models for allosteric
107
proteins. Hemoglobin disorders. Protein folding - denaturation and renaturation. Role of
chaperones. Protein misfolding and aggregation diseases.
UNIT III: Isolation, purification and analysis of proteins No. of hours: 8
Ammonium sulphate fractionation, centrifugation dialysis. Ion-exchange chromatography,

molecular sieve chromatography, affinity chromatography. HPLC and FPLC. Gel
electrophoresis: SDS-PAGE, IEF and 2-D electrophoresis.
UNIT IV: Introduction to enzymes, their characteristics and kinetics No. of hours: 12
Nature of enzymes - protein and non-protein (ribozyme, abzymes). Cofactor and prosthetic
group, apo- and holo-enzymes. Features of enzyme catalysis. Classification of enzymes and
nomenclature. Fischer’s lock & key and Koshland’s induced fit hypothesis. Enzyme
specificity. Enzyme kinetics- Michaelis-Menten equation, Lineweaver-Burk plot.
Determination of Km, Vmax, Kcat. Factors affecting enzyme activity. Enzyme inhibition-
Reversible (competitive, uncompetitive, non-competitive) and irreversible inhibition.
Mechanism based inhibitors.
UNIT V: Mechanism of enzyme action and enzyme regulation No. of hours: 10
General mechanisms of action. Acid-base and covalent catalysis (chymotrypsin, lysozyme).

Metal activated enzymes and metalloenzymes. Allosteric regulation and feedback inhibition
(ATCase). Reversible covalent modification (glycogen phosphorylase). Proteolytic cleavage-
zymogen. Multienzyme complex. Coenzymes.
UNIT VI: Applications of enzymes No. of hours: 8
Isoenzymes. Applications of enzymes in research. Application of enzymes in diagnostics

(SGPT, SGOT, creatine kinase), Enzyme immunoassay (HRP), Enzyme therapy
(Streptokinase). Enzyme immobilization and its applications. Industrial applications.
PRACTICALS
CREDITS: 2 TOTAL HOURS:60
1. Estimation of proteins by Biuret and Lowry methods

2. Ammonium sulphate fractionation of crude homogenate from germinated mung beans
3. Enzyme activity assay (acid phosphatase)
4. Progress curve of enzyme
5. Effect of pH / temperature on enzyme activity
6. Determination of Km and Vmax using Lineweaver-Burk plot.
2.3 References
1. Cooper, T. G. (2011). The Tools of Biochemistry (2nd ed.). Wiley-Interscience

Publication (New Delhi). ISBN: 13:9788126530168.
2. Nelson, D.L. and Cox, M.M. (2017). Lehninger: Principles of Biochemistry (7th ed.).
W.H. Freeman & Company (New York), ISBN:13: 9781464126116 / ISBN:10-
1464126119.
108
3. Nicholas, C.P., Lewis, S. (1999). Fundamentals of Enzymology (3rd ed.). Oxford
University Press Inc. (New York), ISBN: 0 19 850229 X.
4. Sheehan, D. (2009). Physical Biochemistry (2nd ed.). Wiley-Blackwell (West Sussex),
ISBN: 9780470856024 / ISBN: 9780470856031.
5. Voet, D., Voet, J., Pratt, C. (2013). Biochemistry (4th ed.) Wiley & Sons, Inc. (New
Jersey). ISBN: 978-1-11809244-6.

I Students will gain Students will be taught Oral questions will be

knowledge about the using power point asked in the class.
building blocks of proteins presentations, chalk and Assignment and tests
i.e. amino acids and board. In class oral will be given.
understand about the discussion sessions will be
structural organization of conducted.
proteins.
II Students will understand They will be taught using Internal assessment will
about the characteristics of power point presentations, be done on the basis of
tertiary and quaternary chalk and board. The use quiz and class tests.
structures, 3D structure of of E-learning
Hemoglobin and through online Web
Myoglobin. They will also and Video courses will be
understand the concept of included.
protein folding
(denaturation and
renaturation).
III Students will acquire Students will be taught Students will be assigned
knowledge about the basic using chalk and board. different techniques and
concepts of various A visit to a Research Lab. will be asked to deliver a
techniques used for for the demonstration/ power point presentation.
isolation, purification and hands-on-experience of Various analytical
analysis of proteins. protein purification problems will be
techniques will be planned assigned to students
to enhance their ability of related to purification of
learning and imbibing the proteins.
basic concepts.
IV Students will learn about They will be shown power Regular question- answer
enzyme catalysis, role of point presentations and sessions in class will be
coenzymes, cofactors and will be taught using chalk conducted. Internal
different aspects of and board. The use of E- assessment will include
enzyme kinetics. They learning through online problems/ numericals
will understand about Web and Video courses based on enzyme
different types of enzyme will be included for the kinetics.
inhibitors, role of drugs as
109
enzyme inhibitors and the better understanding of the
respective mechanism. enzyme kinetics.
V Students will understand Students will be shown They will be assessed on
the basic mechanism of power point presentations the basis of assignments
enzyme action and and will be taught using and class tests.
enzyme regulation. chalk and board. Oral
discussion sessions in the
class will be conducted.
VI Students will learn about Teaching using chalk and Students will undergo
diverse applications of board will be done. Oral internal test for the
enzymes in research, discussion sessions in the syllabus covered in Unit
diagnostics, therapy and class will be conducted. 1-V and their answers
Industry. will be discussed in the
following class.
Quiz will be conducted.
Various analytical
problems will be
assigned to students
based on enzyme
applications.
4. Keywords
Proteins, Enzymes, Protein structure, Protein folding, Enzyme kinetics, Enzyme

regulation
110
Biochemical Correlations of Diseases (BCH GE-4)
Semester – II / IV
1. Course Objective
This course provides students with knowledge and understanding of various human
diseases. It will introduce the concepts of a well-balanced diet, healthy lifestyle, biochemical
basis of diseases, treatment strategies, mechanism of action of drugs and drug resistance against
various antimicrobials. The course also aims to outline the various strategies that are employed
for preventing infectious and non-infectious diseases.
 Students will develop understanding about the importance of balanced diet, regular
exercises and healthy lifestyle.
 Students will gain insight into various disorders associated with imbalanced diet and
poor lifestyle.
 Students will learn various strategies employed for preventing various human diseases.
 Students will understand the molecular basis of microbial pathogenicity, drug
resistance and implications in public health management.
 Students should be able to handle and solve analytical problems related to theory
classes.
2.2 Course Contents
THEORY
UNIT I: Inherited metabolic diseases No. of hours: 8
Alkaptonuria, Phenylketonuria, Glycogen storage diseases: Von Gierke, Cori and McArdle,
Lipid storage diseases: Gauchers diseases, Niemann-Pick disease, SCID: Adenosine
Deaminase deficiency.
UNIT II : Nutritional deficiency and lifestyle based diseases No. of hours: 16
Kwashiorkar, Marasmus, Beri-beri, Scurvy, Pellagra, Anaemia, Night blindness, Rickets,

Osteomalacia, Osteoporosis, Obesity, Cardiovascular diseases, Atherosclerosis, Diabetes
Mellitus-II, Inflammatory Bowel Disease (IBD).
UNIT III: Hormonal imbalances No. of hours : 8
Hormonal imbalances leading to disease: Diabetes Insipidus, Acromegaly, Gigantism,

Dwarfism, Goitre, Cretinism, Cushing and Conn’s syndrome, Addison’s disease.
111
UNIT IV: Autoimmune diseases No. of hours: 8
Concepts in immune recognition-self and non-self-discrimination, organ specific autoimmune

diseases-Hashimoto’s thyroiditis, Graves’ disease, Myasthenia Gravis, Diabetes Melitus-I,
Systemic diseases: Systemic lupus erythematosus (SLE), Rheumatoid arthritis.
UNIT V: Diseases caused due to misfolded proteins No. of hours: 6
Alzheimer’s, Huntington’s diseases, Kuru, Creutzfeldt-Jakob disease, Sickle Cell anaemia,

Thalassemia.
UNIT VI: Infectious diseases No. of hours: 16
Viral infection: Polio, Measles, Mumps, influenza, HIV. Bacterial infections: Tetanus,
Diphtheria, Tuberculosis, Typhoid, Cholera. Protozoan: Malaria and Trypanosomiasis.
Parasitic infections: Leishmania.
PRACTICALS
1. Determination of blood Lipid Profile: Triglyceride, Cholesterol

2. Anthrompometric measurements: BMI, Waist/Hip Ratio, Mid Arm Muscle Area
(MAMA), Mid Arm Area (MAA).
3. Haemoglobin estimation
4. Blood pressure measurement
5. Calcium estimation in serum
6. Estimation of blood glucose
2.3 References
1. Berg, J.M., Tymoczko, J. L., Stryer, L. (2012). Biochemistry (7th ed.). W.H Freeman
and Company (New York).
2. Coico, R., Sunshine, G. (2009). Immunology: A Short Course (6th ed.). John Wiley &
Sons, Inc (New Jersey). ISBN; 978-0-470-08158-7.
& Sons, Inc. (New York). ISBN: 978-0-4710-28173-4.
4. Prescott, Harley, Wiley, J.M., Sherwood, L.M., Woolverton, C.J. (2008). Klein’s
Microbiology. (7th ed.). Mc Graw Hill International Edition (New York) ISBN: 978-
007-126727.
5. Snustad, D.P., Simmons, M.J. (2012). Genetics (6th ed.). John Wiley & Sons.
(Singapore) ISBN: 978-1-118-09242-2.
112

I. The students will Traditional chalk and board Students will be assigned
understand the concepts method and illustrations the task of identifying
of metabolism of through powerpoint examples of abnormal
macromolecules and the presentations. Discussion of enzymes that directly
diseases related to case studies. Estimation of relate to each feature of
metabolic errors. Glucose, Calcium and metabolic disorders.
Biochemical basis of Blood pressure A host of characteristics
diseases related to measurement will be taught and features will be
inherited metabolic in the practicals. provided to students and
disorders will also be they will need to match
learned. them with the type of
metabolic disorder.
They will encouraged to
participate in group
discussions related to
topics thought in class.
II. Develop understanding Explaining each topic Group discussions and

of the importance of through power point class tests will be held.
balanced diet, regular presentations / chalk and Assignments on
exercises and healthy board teaching. Discussion classification of diseases in
lifestyle and disorders of case studies. various macromolecule
associated with and micromolecule
imbalanced diet and deficient disorders.
poor lifestyle. Signs and symptoms of
Appreciate the diseases will be provided
importance of and students will be asked
micronutrients and to match them with the
disorders associated type of nutrient disorders.
with deficiency of Students will also be given
minerals and vitamins assignments on matching
The students will also the symptoms with the
learn about life style diseases.
disorders.
III. Learn about role of Class teaching using chalk Students will be given
hormones in our daily and board and power point assignments to match
life and gain insight into presentations. symptoms with the correct
various diseases disease/ disorders.
associated with Group discussions and
hormonal imbalance. Tests will be held.
IV The students will learn Traditional chalk and board Pre-lecture quiz to
about induction of an method with powerpoint evaluate student’s
appropriate immune presentations. understanding of previous
response and the Few case studies will also lecture. Signs and
113
associated disorders, be discussed. symptoms of diseases will
also understand the be provided and students
concept of immune will be asked to classify
recognition - self and them in various types of
nonself. autoimmune diseases.
V. Understand the Illustrations through power Group discussions. Quiz,
significance of point presentations and Assignments. Signs and
appropriate folding of through regular chalk and symptoms of diseases will
proteins and the board method. Discussion be provided and students
diseases caused due to of case studies. will be asked to classify
misfolding of proteins. them in diseases caused by
misfolding of proteins.
Internal assessment test.
VI. Gain knowledge about Traditional chalk and board Pre-lecture quiz to
various microbial method with powerpoint evaluate student’s
infectious agents that presentations. understanding of previous
cause diseases in lecture.
humans. Students will Assessment tests (end-
gain insight into host term) will be conducted.
immune responses that Students will be assigned
ensue following various topics and will be
infection. asked to deliver a
powerpoint presentation
on the assigned topics.
4. Keywords
Lifestyle and metabolic disorders, nutritional deficiency, hormonal disorder,

autoimmunity and infectious diseases.
114
Intermediary Metabolism (BCH GE-5)
Semester - III
The objective of this course is to provide the students an understanding of the major
metabolic pathways associated with biomolecules within a cell and their regulation. It will also
provide knowledge about the possible correlation between various metabolic pathways.
At the end of the course, the students will be able to:
 Understand the basics of metabolic pathways

 Outline the pathways involved in catabolism and biosynthesis of glucose.
 Describe the mechanism of ATP synthesis.
 Understand the biosynthesis and degradation of glycogen
 Comprehend the metabolism of fatty acids, amino acids, and nucleotides
 Develop an understanding of metabolic integration
2.2 Course Contents
THEORY
UNIT I: Glycolysis and gluconeogenesis No. of hours: 12
Nature of metabolism. Role of oxidation and reduction and coupling of these. ATP as energy
currency. Glycolysis a universal pathway, fructose and galactose oxidation, anaerobic
glycolysis, fermentation, gluconeogenesis, reciprocal regulation of glycolysis and
gluconeogenesis. Pentose phosphate pathway, importance of various pathways and their
regulation
UNIT II: Citric acid cycle and oxidative phosphorylation No. of hours: 12
Pyruvate dehydrogenase complex, oxidation of acetyl CoA, amphibolic role, regulation and
glyoxylate pathway. The respiratory chain in mitochondria, proton gradient powering ATP
synthesis, glycerol-3-phosphate and malate-aspartate shuttle, regulation of oxidative
phosphorylation.
UNIT III: Glycogen metabolism No. of hours: 8
Glycogenolysis, phosphorylase regulation, role of epinephrine and glucagon for

glycogenolysis, glycogenesis; reciprocal regulation of glycogenesis and glycogenolysis.
Diseases associated with the abnormal carbohydrate metabolism.
115
UNIT IV: Fatty acid and amino acid degradation No. of hours: 12
TAG as energy source, β oxidation of fatty acids in mitochondria and peroxisomes, ketone
bodies. Fatty acids activation, regulation of fatty acid oxidation, Protein degradation to amino
acids, Role of essential and non-essential amino acids in growth and development. Protein
calorie malnutrition - Kwashiorkar and Marasmus, urea cycle, feeder pathways into TCA cycle.
Nitrogen fixation. Diseases associated with the abnormal metabolism.
UNIT V: Nucleotide metabolism No. of hours: 10
Biosynthesis - de novo and salvage pathways, regulation of nucleotide synthesis by feedback

inhibition, degradation and excretion. Diseases associated with the abnormal metabolism
UNIT VI: Integration of metabolism No. of hours: 6
Brief role of hormones - insulin, glucagon; metabolic shifts to provide fuel to brain during
fasting and starvation, Increase in gluconeogenesis and muscle protein breakdown.
PRACTICALS
1. Estimation of blood glucose

2. Demonstration of alcohol fermentation by yeast.
3. Estimation of serum urea.
4. Estimation of serum uric acid.
5. Estimation of serum creatinine
2.3 References
1. Berg, J.M., Tymoczko, J.L., Stryer L., (2012) Biochemistry7th ed., W.H. Freeman and
Company (New York); ISBN:10:1-4292-2936-5, ISBN:13:978-1-4292-2936-4.
2. Campbell, M.K., Farrel, S.O. (2012) Biochemistry7th ed, S.O. Brooks/Cole, Cengage
Learning (Boston); ISBN: 13:978-1-111-42564-7 ISBN:10:1-4292-2936-5.

I. Understanding the Traditional chalk & board Post lecture students will
concept of method with power-point be given home
metabolism. presentations. assignments to enhance
Understand their learning and for
Glycolysis, assimilation of concepts.
gluconeogenesis and
Pentose phosphate
pathway and their
regulation.
116
II. Understand the citricRevision of the previous Pre-lecture quiz to
acid cycle and ATP classes will be conducted. evaluate students
synthesis by Teaching will be through understanding of previous
oxidative traditional chalk & board lecture. Internal
phosphorylation. method and power-point assessment tests will be
presentations conducted.
III. Have knowledge Group discussions will be held Home assignments and
about glycogenolysis on various topics of this unit. MCQ based questions will
and glycogenesis and Blackboard teaching as well as be given to students.
their reciprocal powerpoint presentations will
regulation be conducted.
IV Understand the β- Traditional chalk & board Pre-lecture quiz to
oxidation of fatty method with power-point evaluate students
acids and its presentations. Oral question- understanding of previous
regulation. answers will be held. lecture. Students will be
asked to deliver
presentations and will be
assessed on that.
V. Understand de novo Oral revision of the previous Internal assessment test
and salvage classes will be conducted. and crossword puzzles will
pathways of Teaching will be through be given to students for
nucleotide traditional chalk & board their evaluation.
Biosynthesis and method with power-point
Degradation. presentations.
VI. Understand the Overview of all the metabolic A continuous evaluation
concept of metabolic pathways will be discussed based on their class
integration. along with group discussions. response will be made.
Traditional chalk & board End term examination
method with power-point evaluation. MCQ based
presentations. questions.
4. Keywords
Glycolysis, De novo salvage pathway, TCA, catabolism, anabolism, integrative

pathways, nucleotide metabolism, beta oxidation, glycogen metabolism, gluconeogenesis.
117
Biochemical Applications in Forensics (BCH GE-6)
Semester – III / IV
The course aims to provide an understanding of the applications of biochemistry in
forensic sciences through analysis of evidences, which will help students develop analytical
and problem solving skills for real life situation. The course will keep abreast with all recent
developments and emerging trends in forensic science thus helping interested students take up
forensic science as future course of study.
 Students will learn the fundamental concepts and principles of forensic science and
their significance.
 Students will understand how a forensic investigation is initiated through preservation
of evidences, as well as chemical, physical and biological methods of their analysis
including analysis of DNA and other bodily fluids.
 Students will learn how to establish identity of an individual by document
evaluation, fingerprints, footprints and DNA analysis.
 Students will obtain hands-on-experience in some of the basic biochemical processes
involved in forensic investigation.
2.2 Course Contents
THEORY
UNIT I: Introduction to forensic sciences No. of hours: 10
Basic Principles and Significance; History and Development of Forensic Science; Defining the
scene of investigation; Collection, Packaging, Labelling and Forwarding of biological exhibits
to forensic laboratories; Preservation of biological evidence; Importance of Health and Safety
Protocols in sample collection and analysis.
UNIT II: Biological science and its application in investigation No. of hours: 20
Biochemical analysis of various biological evidences like blood, semen & other biological
fluids, viscera, bite marks, hair (animal and human), fibers & fabrics, pollen and soil;
Establishment of identity of individuals - fingerprints, footprints, blood and DNA analysis,
anthropology – skeletal remains, Odontology; Time of death - rigor mortis, liver mortis, algor
mortis, forensic entomology. Biochemical basis for determination of cause of death, case
studies
118
UNIT III: Chemical science and its application in investigation No. of hours: 15
Detection of drugs of abuse and narcotics in biological samples; Toxicological examination of

viscera, detection of petroleum products, food adulteration; Analysis of inks and their use in
questioned document identification, blood splatter analysis, stain analysis, case studies.
UNIT IV: Recent advances in forensics No. of hours: 15
Narco analysis: theory, forensic significance, future prospect; Brain mapping: introduction,
EEG, P-3000 wave, forensic applications, limitation of technique; Polygraph: Principle and
technique, polygraph as forensic investigative tool, use of psychoactive drugs in forensic
analysis. NHRC guidelines for polygraph test; Facial reconstruction: Method and technique,
facial reconstruction in forensic identification; DNA Finger Printing; DNA-Introduction,
source of DNA in Forensic case work, Extraction of DNA, Techniques of DNA fingerprinting-
RFLP, STR, PCR. DNA fingerprinting in paternity disputes, mass disaster and other forensic
case work, case studies.
PRACTICALS
1. TLC method for differentiation of ink/drugs

2. Fingerprint development from various surfaces
3. Handwriting identification based on class characteristic and individual characteristics
4. Microscopic examination of hair/fiber/pollen/diatom
5. Examination of blood samples: Blood grouping, DNA finger printing, Blood splatter
analysis.
6. Examination of urine samples: Identification of drugs.
7. Field trip to a forensic laboratory.
2.3 References
1. James, S. H., Nordby, J. J. & Bell, S. (2014). Forensic Science: An Introduction to

Scientific and Investigative Techniques, Fourth Edition: Taylor & Francis. ISBN
9781439853832
2. Jones, P., & Williams, R. E. (2009). Crime Scene Processing and Laboratory Workbook
First Edition: CRC Press. ISBN 9780429249976
3. Lee, H., Palmbach, T. & Miller, M. (2001). Henry Lee's crime scene handbook, First
Edition: Academic Press ISBN 9780080507989
4. Parikh, C. K. (2016). Parikh's textbook of medical jurisprudence, forensic medicine and
toxicology : for classrooms and courtrooms, Seventh Edition: CBS Publishers and
Distributors. ISBN 9788123926469
5. Saferstein, R. (2018). Criminalistics: An Introduction to Forensic Science, Twelveth
edition: Pearson Education. ISBN 10:0134477596, ISBN 13: 9780134477596
6. Tewari, R. K., Sastry P. K., Ravikumar, K. V. (2002). Computer Crime and Computer
Forensic, First Edition: Selective & Scientific Books
7. Veeraraghavan, V. (2009). Handbook of Forensic Psychology, First Edition: Selective
& Scientific Books
119

No. Activity
I. Comprehend the developments Teaching will be conducted Internal
in the field of forensic sciences, both through black board assessment tests.
learn to observe a crime scene mode and power point Students will be
for identification of relevant presentation mode. given questions
evidences and samples for Discussions and quizzes that are application
forensic analysis. Understand will be conducted to keep based and require
the importance of collection, the students up-to-date with analytical skills
packaging and preservation of the information they have
samples to ensure reliability of received and to gauge their
data generated. conceptual understanding.
Use models of crime scenes
for practical training on
sample identification and
collection.
II. Understand the importance of Class teaching with black Conduct of
precision, reproducibility and board and power point Internal
accuracy in identification of a presentation modes. assessment tests.
biological sample. Learn the Discussions on case studies PowerPoint
methods to identify the and quizzes will be presentation on the
accurate age, sex and identity conducted to keep the assigned topics.
of an individual and identify students up-to-date with the
time and cause of death in a information they have
forensic investigation. received and to gauge their
conceptual understanding.
Practical training on
microscopic identification
of various biological
samples, finger print
development from surfaces
and identification of
fingerprints.
III. Gain knowledge about the Power point presentation Internal
methods used to analyse will be used to teach various assessment tests
samples for drug testing, ink methods. Use of blackboard will be conducted.
and stain testing and document and general discussions in Analyzing case
and handwriting verification. the class. Practical analysis studies. Open
of urine samples for drug book tests to
tests. Practical analysis of promote self-
inks and stains. learning.
IV Understand the physiology and Teaching using chalk and Internal
biochemistry behind tests like board and video tutorials. assessment tests
Narcoanalysis, polygraphy, lie will be conducted.
detection and facial Expert lecture on course A PowerPoint
reconstruction. Also, learn the related topics and filed trip presentation on
120
importance of DNA to labs. Practical exercises any interesting
fingerprinting in forensic on DNA fingerprinting. case study and the
investigations use of forensic
technology in
investigation.
Practical record
book assessment,
oral discussion and
question- answer
sessions on
practical topics.
4. Keywords
Forensic biology; blood splatter analysis; toxicology; narco-analysis; DNA

fingerprinting; polygraph; odontology; forensic entomology.
121
Recombinant DNA Technology (BCH GE-7)
Semester - IV
1. Course Objectives:
The objective of the course is to teach basics of theory and practical aspects of
recombinant DNA technology and the various techniques for DNA manipulation in
prokaryotes and eukaryotes. The course will also outline the applications of this knowledge for
the development of diagnostics, therapeutics and vaccines.
2.1 Course Learning Outcomes:
The students after completing this course will be able to understand:
 Principles and importance of gene cloning

 Various methods for screening of recombinants and identification of cloned gene
 Polymerase chain reaction and DNA sequencing
 Recombinant gene expression system
 Application of recombinant technology in the production of Biopharmaceutical
processes and products such as insulin, vaccines and DNA finger printing.
THEORY
UNIT I: Introduction to recombinant DNA technology No. of hours: 8
Overview of gene cloning. Restriction, modification systems and DNA modifying enzymes,
DNA analysis by electrophoresis.
UNIT II: Cloning vectors for prokaryotes and eukaryotes No. of hours: 12
Plasmids and bacteriophages as vectors for gene cloning. Cloning vectors for E. coli like
pBR322, pUC8, pGEM3Z. Cloning vectors based on M13 and λ bacteriophage. Ti plasmid,
BAC and YAC.
UNIT III: Introduction of DNA into cells and selection of recombinants No. of hours: 12
Ligation of DNA molecules. Introduction of DNA into cells, Transformation, selection for
transformed cells. Identification of recombinants, blue-white selection. Identification of
recombinant phages. cDNA and Genomic libraries.
UNIT IV: Polymerase chain reaction and DNA sequencing No. of hours: 08
Fundamentals of polymerase chain reaction, designing primers for PCR. DNA sequencing by
Sanger’s method and automated DNA sequencing.
122
UNIT V: Expression of cloned genes No. of hours: 12
Vectors for expression of foreign genes in E. coli, cassettes and gene fusions. Production of
recombinant protein by eukaryotic cells. Fusion tags and their role in purification of
recombinant proteins.
UNIT VI: Applications of genetic engineering in biotechnology No. of hours: 12
Production of recombinant proteins such as insulin and factor VIII. Gene therapy. Genetically
modified herbicide glyphosate resistant crops. Ethics concerns.
PRACTICALS
1. DNA estimation by UV spectrophotometry.

2. Isolation of plasmid DNA from E. coli.
3. Restriction digestion and agarose gel electrophoresis.
4. Amplification of a DNA fragment by PCR.
2.3 References
1. Brown, T. A. (2016) Gene Cloning and DNA Analysis: An Introduction, (7th ed.).
Wiley-Blackwell Publishing (Oxford, UK); ISBN: 978-1-119-07256-0
2. Glick, B.R., Pasternak, J.J., Patten, C. L. (2010) Molecular Biotechnology: Principles
and Applications of Recombinant DNA (4th ed.). ASM Press (Washington DC); ISBN:
978-1-55581-498-4.

I. Students will be Teaching will be MCQ tests,
introduced to purpose and conducted through both assignments,
importance of gene black board mode and Analytical questions
cloning, Restriction, power point presentation
modification systems and mode. They are also
DNA modifying enzymes, encouraged to attend the
DNA analysis by practicals for the better
electrophoresis. understanding of the
techniques.
II. Students will gain insight Students will be asked to Students will be given
of different vectors used orally revise the previous assignment on different
for gene cloning like class before every new topics and will be asked
pBR322, pUC8, pGEM3Z, class helping them in to deliver a power-point
123
Cloning vectors based on better understanding and presentation on the
M13 and λ bacteriophage. their doubts cleared, if applications of vectors,
Plant vectors like Ti any. Regular classroom MCQ tests and quizzes
plasmid, high capacity teaching, visual aids, to assess regular
vectors like BAC and discussions understanding of the
YAC. topic
III. Students will learn in Students will be asked to Mid-term tests will be
detail about Ligation of orally revise the previous conducted.
DNA molecules into class before every new
vectors, Introduction of class helping them in
recombinant DNA into better understanding and
host cells, Transformation, their doubts cleared, if any.
selection for transformed Teaching will be
cells. Identification of conducted through both
recombinants through black board mode and
blue-white selection. power point presentation
Identification of mode.
recombinant phages. Gene
libraries.
IV Students will gain insight Students will be asked to Assignments and
of principle of polymerase orally revise the previous presentations ,
chain reaction, designing class before every new analytical problems and
primers for PCR.DNA class helping them in class tests
sequencing by Sanger’s better understanding and
method and automated their doubts cleared, if any.
DNA sequencing. Teaching will be
conducted through both
power point presentation
mode.
V. Students will learn about Presentations, Classroom Presentations and
the Vectors used for Teaching, connect with assignments
expression of foreign practicals, discussions
genes in E. coli, cassettes
and gene fusions.
Production of recombinant
protein by eukaryotic cells.
Fusion tags and their role
in purification of
recombinant proteins
VI. Students will gain Visual aids, Presentations, Internal assessment test
knowledge about the Classroom Teaching and (end term) will be
various application of discussions. conducted.
recombinant DNA
technology through
various examples like
Production of recombinant
proteins such as insulin
and factor VIII. Gene
therapy. Genetically
124
modified herbicide
glyphosate resistant crops.
Ethics concerns.
4. Key Words
Genetic Engineering, Recombinant Proteins, Biotechnology
125
SKILL ENHANCEMENT ELECTIVE (SEC) COURSES
126
Biochemical Techniques (BCH SEC-1)
Semester - III
The objective of the course is to introduce to the students, various techniques that are
used in a biochemistry lab and to provide them with an understanding of the principle
underlying these techniques and laboratory skills in the form of practical exercises so that
students can apply this knowledge to pursue research.
The course is designed for undergraduate students to learn the basic concepts of various
techniques used in Biochemistry. The course will enable students to:
 Acquire knowledge about the principles and applications of spectrophotometric and

chromatography techniques used in a biochemistry lab.
 Learn about the principle and applications of electrophoresis and centrifugation
techniques.
 Obtain hands-on-experience and laboratory skills expected of any biochemist working
in a research lab.
THEORY
UNIT I: Spectroscopic Techniques No. of hours: 6
Electromagnetic radiation, interaction of radiation with biomolecules, principle of UV-visible

absorption spectrophotometry, Lambert's Law, Beer's Law, Working of a spectrophotometer.
Applications of UV-visible absorption spectrophotometry in Biochemistry. Fluorescence
spectrophotometry and its applications in biochemistry.
UNIT II: Chromatography No. of hours: 10
Introduction to chromatography. Principle and applications of Paper Chromatography, Thin

Layer Chromatography, Ion-Exchange Chromatography, Gel filtration and Affinity
Chromatography.
UNIT III: Electrophoresis No. of hours: 8
Principle of electrophoresis, Polyacrylamide gel electrophoresis (native and denaturing) for

proteins and nucleic acids. Agarose gel electrophoresis, Isoelectric focusing of proteins, two-
dimensional. Detection and identification of proteins and nucleic acids and determination of
molecular weight.
127
UNIT IV: Centrifugation No. of hours: 6
Principle of centrifugation, basic rules of sedimentation, sedimentation coefficient. Various

types of centrifuges, types of rotors. Application of centrifugation, differential centrifugation,
density gradient centrifugation (zonal and isopycnic).
PRACTICALS
1. Determination of absorption maxima (λmax) of small molecules and macromolecules.

2. Verification of Beer’s Law.
3. Determination of molar extinction coefficient.
4. Separation of amino acid acids/sugars by thin layer chromatography (TLC)
5. Separation of proteins by gel filtration chromatography
6. Separation of proteins by ion-exchange chromatography
7. Separation of nucleic acids using agarose gel electrophoresis
8. Separation of protein by SDS-PAGE.
2.3 References
1. Boyer, R. F. (2012) Biochemistry Laboratory: Modern Theory and Techniques, (6th

ed.), Boston, Mass: Prentice Hall; ISBN-13: 978-0136043027.
2. Plummer, D. T. (1998) An Introduction to Practical Biochemistry (3rd ed.), Tata
McGraw Hill Education Pvt. Ltd. (New Delhi); ISBN: 13: 978-0-07-099487-4 /
ISBN:10: 0-07-099487-0.
3. Wilson, K. & Walker J (2010) Principles and Techniques of Biochemistry and
Molecular Biology, (7th ed.), Cambridge University Press; ISBN 978-0-521-51635-8.
Additional Reading
1. Cooper, T. G. (2011) The Tools of Biochemistry (2nd ed.), Wiley-Interscience

Publication (New Delhi); ISBN: 13:9788126530168.
2. Freifelder, D. (1982) Physical Biochemistry: Applications to Biochemistry and
Molecular Biology, (2nd ed.), W.H. Freeman and Company (New York); ISBN:0-7167-
1315-2 / ISBN:0-7167-1444-2.

I Students will learn about Teaching using chalk Problems will be
the principle and and board; Oral assigned related to
applications of discussion sessions in Beer’s Law and
spectrophotometry and the class. Powerpoint Lambert’s Law to test
flourimetry. presentations. the understanding of
students.
128
II Students will learn the Teaching using chalk Practical exercises are
principle of various and board; Oral designed whereby the
chromatographic discussion sessions in students get hands on
techniques like gel the class. Powerpoint experience with these
filteration, Ion exchange. presentations. chromatography
techniques.
III Students will learn about Power point Various analytical
electrophoretic techniques, presentations; Teaching problems will be
their principle and using chalk and board; assigned to students
applications in analyzing Oral discussion sessions related to
proteins and nucleic acids in the class electrophoretic
separation.
IV Students will learn about Power point Demonstration with the
the basic rules of presentations; Teaching help of centrifuges and
sedimentation, various using chalk and board; rotors to improve their
types of centrifuges and Oral discussion sessions understanding.
rotors. in the class
4. Keywords
Spectrophotometry, Chromatography, Proteins, Nucleic Acids, Centrifugation and

Electrophoresis
129
Biostatistics (BCH SEC-2)
Semester - III
The primary objective of this course is to provide understanding about the principles
of biological data collection, statistical analysis and presentation. The course will also provide
hands-on-experience through practicals that are well correlated with the theory topics and are
designed to support skill oriented learning outcomes in the management of biological data.
Learners will be able to:
 Understand the principles of biological data collection, statistical analysis and

presentation.
 Appreciate various factors that influence the type of sample collected and sample size.
 Analyze and interpret biological data using appropriate statistical tools
 Apply the principles of biological data management in real life situations
 Improvise their computational, mathematical and computer skills, which would
increase their eligibility to pursue research based higher education.
THEORY
UNIT I: Data Collection and Presentation No. of hours: 4
Importance of statistical analysis in biological data management. Sampling schemes – Simple

Random sampling, Systemic sampling, Stratified sampling, Cluster sampling, Non probability
sampling; Types of numerical data – nominal data, ordinal data, ranked data, discrete data,
continuous data; Modes of presenting data: Frequency distributions, Relative frequency.
UNIT II: Measures of central tendency and analysis of variance No. of hours: 12
Mean, median, mode; Co-efficient of variation and standard deviation; Range and interquartile
range; Grouped mean and grouped variance; Frequency distributions; One way ANOVA; Two-
way ANOVA; AMOVA; student’s t test
UNIT III: Probability No. of hours: 4
Operations on events, Venn diagrams, Conditional Probability; Probability distributions.
UNIT IV: Hypothesis Testing No. of hours: 4
General concepts – Null hypothesis, alternative hypothesis, Rejection of hypothesis; Type I

and Type II errors; P value and sample size estimation.
130
UNIT V: Regression and Correlation No. of hours: 6
Chi Square Test – Observed and expected frequencies, Calculating p values, assumptions of a
chi square goodness of fit; Correlation –Two-way scatter plot, Pearson’s correlation
coefficient; Regression – regression concepts, simple linear regression; Calculation of R2 and
ρ.
PRACTICALS
1. Collection of data - Random sampling method; Stratified sampling method; Cluster

sampling method
2. Data representation - Frequency and relative frequency distribution table, Plotting
different biological data in a best representative graphical format.
3. Data analysis - Calculating Mean, median, mode, variance, standard deviation and
standard error for a given data set. Standard t-test for grouped samples. Analysis of 2
way variance
4. Chi square goodness of fit test. Regression analysis and calculating regression
coefficient
5. Learning to analyze data using SPSS or R software
6. Project assignment.
2.3 References
1. Michael, C.W. (2015) The Analysis of Biological Data (2nd ed.), Macmillan
Publishers, ISBN-10: 1-936221-48-9; ISBN-13: 978-1-936221-48-6
2. Pagano, M . and Gauvreau , K .(2018) Principles of Biostatistics (2nd ed.), Chapman
and Hall/CRC; ISBN 9781138593145
1. Zar, J.H. (2010) Biostatistical analysis, (5th ed.), Pearsons Int. Edition; ISBN- 978-0-
13-206502-3.

No. Activity
I. Understand the principles of Teaching will be Internal assessment
biological data collection and conducted both through tests.
presentation. Learn and black board mode and Students will be given
appreciate various factors that power point presentation questions that are
mode. Exercises on application based and
131
influence type of sample Collection and require analytical
collected and sample size. presentation of data. skills
Field exercises on
collection of data
II. Analyze and interpret Teaching will be Conduct of Internal
biological data using simple conducted both through assessment tests
statistical tools like mean, black board mode and Students will be given
median, mode, variance and power point presentation questions that are
standard deviation. Apply the mode. application based and
principles of biological data Exercises on statistical require analytical and
management in real life analysis of biological computational skills
situations data. Learning to analyze
Improve their computational, data using SPSS or R
mathematical and computer software
skills by learning to use
ANOVA,AMOVA and student
t-test on free access statistical
software
III. Understand the concept of Teaching will be Students will be given
probability and the importance conducted both through MCQ based tests and
and use of probability in black board mode and quiz
analyzing biological data. power point presentation
mode.
IV Learn and appreciate various Teaching will be Formulate a
factors that influence stating conducted both through hypothesis on any
and formulating a hypothesis, black board mode and are/topic of interest,
relevance to type of sample power point presentation determine appropriate
collected and sample size. mode. sample size and collect
Analyzing case studies to data.
understand hypothesis
formulation
V Understanding how to manage Teaching will be Internal assessment
data for a goodness of fit chi- conducted both through tests will be
square test versus an black board mode and conducted.
interdependence chi-square power point presentation Analyze data collected
test. mode. Exercises on using appropriate
Learn and appreciate various statistical analysis of statistical tools and
factors that influence the use biological data. Learning present the data.
of correlation and regression to analyze data using
analysis for biological data. SPSS or R software
4. Keywords
Statistical analysis, biological data collection, sampling, data presentation, measures of

central tendency, ANOVA, chi-square, regression
132
Research Methodology (BCH SEC-3)
Semester – III / IV
The main objective of this paper is to provide students with a general introduction to
the methodological foundations and tools used in research for an understanding of the ways to
identify problems, develop hypotheses and research questions and design research projects.
The course will expose students to the range of designs used in research in laboratory, field
experiments, surveys and content analysis. It will also provide an introduction to the concept
of controls, statistical tools and computer applications used in research. In addition, the course
will impart knowledge of scientific writing, oral presentation and the various associated ethical
issues.
2. 1 Course Learning Outcomes:
By studying this paper students will be able to:
 Define research, learn the importance of research and its link with theoretical
knowledge
 Describe the research process and the principle activities, skills and ethics associated
with the research process
 Describe and compare the major quantitative and qualitative research methods
 Construct an effective research proposal
 Understand the importance of research ethics use the computer software for
organization and analysis of data.
 Develop skills in the art of scientific writing and oral presentation
2.2 Course Contents
THEORY
UNIT I: Objectives of research No. of hours: 4
Definition, objectives, types of research, classification, various phases of research.
UNIT II: Research proposals and literature survey No. of hours: 6
Research proposal and aspects, Review of literature using appropriate sources – reviews,
patents, research papers, books.
UNIT III: Basic principles of research design No. of hours: 6
Types of research designs – exploratory, descriptive, experimental, survey and case study.
133
UNIT IV: Experimental, sampling design and data collection No. of hours: 6
Sample - types, criteria, characteristics and steps; Tools and techniques to execute experiments;
Observation, questionnaire, interview
UNIT V: Interpretation, report writing and the art of oral presentation

No. of hours: 4
Report writing, format of publications in research journals, how to present papers and research
findings
UNIT VI: Bioethics and Plagiarism in Research No. of hours: 4
Biosafety and Ethics - compliance and concerns; Plagiarism; Introduction to Intellectual

Property Rights; Citation and acknowledgement
PRACTICALS
1. Writing of a mini-review paper

2. Design of a research survey on a specific problem
3. Idea presentations in small groups
4. Interaction with an expert during special lecture
2.3 References
1. Cresswell, J. (2009) Research Design : Qualitative and quantitative Approaches

Thousand Oaks CA, (3rd ed.), Sage Publications
2. Kothari, C.R. (2004) Research Methodology: Methods and Techniques (2nd ed.), New
Age International Publishers.
3. Kumar, R. (2011) Research Methodology: A Step-by-Step Guide for Beginners (5th ed.),
SAGE publisher
4. Walliman, N. (2017) Research Methods: The Basics, (2nd ed.), London ; New York :
Routledge
5. WHO (2001) Health Research Methodology – A Guide for Training in
Research Methods.

I. Students will be able to Teaching will be conducted Internal assessment tests
define research and through both black board will be conducted. Group
understand its objectives. mode and power point discussions will be
They will recognize the presentation mode. assigned.
various types and classes
of research.
134
II.
Students will gain insight Group discussions; Idea Assign group discussion
about the importance of presentations; Proposing a on specific topics; Will be
Research proposals and research topic; Perform a asked to retrieve literature
literature survey. They will literature survey on the based on a given topic.
be made capable in given/proposed topic Students will be
identifying broad area of encouraged to meet
research and write research departmental faculties and
proposal. They will be able discuss on their successful
to review literature using a research proposals.
wide variety of sources
like web and libraries
III. Students will learn the Group discussions; Internal assessment tests
basic principles of research Design of a proposed will be conducted.
design and its various research topic; Online Report/paper writing will
types. courses on the topic be assigned
IV Students will gain insight Plan the sampling and Internal assessment tests
about the experimental, data collection method of will be conducted. Group
sampling design and data their proposed topic of discussions; Paper
collection. They will learn research. Learn the proper presentation; Seminars
a variety of ways to collect way of data reporting and
the samples. They will be its record keeping
able to devise optional
plans, tools and techniques
for experimental design
and its execution
V. Students will gain Learn the skill of report Will be assigned writing of
knowledge about data and publication writing small reports and defending
interpretation, report in their proposed topic of them orally. They will be
writing and the art of oral research based on input encouraged to present
presentation. They will not from teachers scientific papers as well.
only be able to understand
the format of report
writing but also scientific
publications
VI. Students will learn about Articles on these issues Students will be assigned
the role of bioethics and will be provided to the task of retrieving
plagiarism in Research. students. Classical mode of bioethics, plagiarism,
They will be educated to chalk and board teaching ethical issues related
follow ethics compliance as well as power point policies of the government
and concerns. They will be presentations will be used. or of institutions. They will
educated about the concept Experts in these areas will be assigned the task of
of Citation and be invited to deliver special identifying citations of
acknowledgement lectures. publications of faculties.
4. Keywords
Research methodology; Patents; Plagiarism; Ethics; Biosafety; Report writing
135
Bioinformatics (BCH SEC-4)
Semester - IV
The objective of this course is to impart basic understanding of bioinformatics and

computational biology. The course will introduce the broad scope of bioinformatics by
discussions on the theory and practices of computational methods in biology. This course also
aims to provide students with a practical hands-on experience with common bioinformatics
tools and databases. Students will be trained in the basic theory and application of programs
used for database searching, protein and DNA sequence analysis, and prediction of protein
structures.
After completion of the course, a student will:
 Understand the basics of bioinformatics and computational biology and develop

awareness of the interdisciplinary nature of this field.
 Gain the ability to use several softwares/tools in biology
 Gain confidence to discuss, access and use biological databases in public domain
 Understand protein structure using visualization softwares
 Be able to gain understanding of sequence alignments
 Be able to analyze phylogeny using alignment tools
 Comprehend the fundamental aspects of in-silico protein structure prediction
 Understand how theoretical approaches can be used to analyze biological systems
 Obtain knowledge on applications of bioinformatics from genomes to personalized
medicine.
2.2 Course Contents
THEORY
UNIT I: Introduction to bioinformatics No. of hours: 4
Introduction to Bioinformatics, Computer fundamentals – Operating Systems, Hardware,

Software, Programming languages in bioinformatics - PERL/R programming, role of
supercomputers in biology, Historical background. Scope of bioinformatics - Genomics,
Proteomics, Computer aided drug discovery and design (CADD) and Systems Biology.
UNIT II: Biological databases and data retrieval No. of hours: 8
Introduction to biological databases - primary, secondary and composite databases, NCBI,

nucleic acid databases (GenBank, EMBL, DDBJ, NDB), protein databases (PIR, Swiss-Prot,
136
TrEMBL, PDB), metabolic pathway database (KEGG, EcoCyc, and MetaCyc), small molecule
databases (PubChem, Drug Bank, ZINC, CSD). Organism specific databases (E. coli, yeast,
Arabidopsis, mouse, Drosophila melanogaster), Structure viewers (Ras Mol, J mol) and File
formats.
UNIT III: Sequence alignment & phylogeny No. of hours: 8
Similarity, identity and homology. Concept of Alignment – local and global alignment,
pairwise and multiple sequence alignments, amino acid substitution matrices (PAM and
BLOSUM), BLAST and CLUSTALW, Definition of phylogeny and its importance, Methods
of Phylogenetic tree generation, Phylip
UNIT IV: Genomics No. of hours: 4
Introduction to genomics, comparative and functional genomics, gene structure in prokaryotes

and eukaryotes, Genome annotation, gene prediction approaches and tools.
UNIT V: Protein sequence, structure prediction and analysis No. of hours: 6
Protein Structure - Primary, Secondary and Tertiary structure, Protein structure prediction
methods: Homology modeling, Fold recognition and ab-initio methods, Ramachandran plot.
PRACTICALS
1. Sequence retrieval (protein and gene) from NCBI and Molecular file formats - FASTA,
GenBank/Genpept.
2. Structure download (protein and DNA) from PDB and Molecular viewer by
visualization software ( Pymol / Rasmol/Jmol)
3. BLAST suite of tools for pairwise alignment
4. Multiple sequence alignment (CLUSTALW/TCoffee) and construction of guide trees
5. Gene prediction using GENSCAN/GLIMMER
6. Primary sequence analyses (Protparam) and Secondary structure prediction (GOR,
nnPredict).
7. Tertiary structure prediction (SWISSMODEL) and Protein structure evaluation -
Ramachandran map (PROCHECK
2.3 References
1. Chandra, S.M., Choudhary, K.R. and Mir Asif Iquebal A.M. (2017) Basic Applied
Bioinformatics John Wiley & Sons; ISBN9781119244370
2. Ghosh, Z. and Mallick, B., (2008) Bioinformatics – Principles and Applications, (1st
ed.) Oxford University Press (India), ISBN: 9780195692303.
3. Gromiha, M.M. (2010). Protein Bioinformatics: From Sequence to Function;
Academic Press eBook; ISBN: 9780123884244 Paperback ISBN: 9788131222973
137
4. David M. (2004). Bioinformatics: Sequence and Genome Analysis. Cold Spring
Harbor Laboratory Press; ISBN 978-087969712-9
5. Andreas D., Baxevanis D.A. and Ouellette Francis B.F. (2005), Bioinformatics: A
Practical Guide to the Analysis of Genes and Proteins (3rd ed.), John Wiley & Sons,
Inc. (New Jersey), ISBN: 0-47147878-4.
Additional Reading
1. Krane, D.E. and Raymer, M. L. (2006). Fundamental concepts of bioinformatics,

Pearson Education Inc.; ISBN 10: 0805346333 ISBN 13: 9780805346336
2. Pevsner, J. (2003). Bioinformatics and Functional Genomics (1st ed.), John Wiley &
Sons, Inc. (New Jersey); ISBN: 0-47121004-8.

I. Students will be Outlining history of Discussion of research and
familiarized with the development about review articles and class
concept of Bioinformatics through presentations
Bioinformatics & power point presentations
Computational tools and chalk & board method;
with applications in
biology
II. Students will learn Traditional chalk & board Computer assisted quizzes,
about Biological method with powerpoint assignments. Students will
Databases and the presentations on biological be assigned a topic and
types of databases. databases asked to search for
They will also databases associated to the
understand various topic
file formats used for
sequence and structure
analysis
III. Students will learn Chalk and board and notes; Class presentations and
about sequence Power point presentations assignments will help
alignment methods. for images for clarity of students understand
Pairwise and multiple concepts; Research papers phylogeny
sequence alignment will be discussed
will be discussed in
detail with examples of
BLAST and
CLUSTALw. They
will also learn methods
for phylogeny
IV Students will Power point presentations; Assignments & Quiz
understand different Chalk and board; Student
138
applications of interaction in class
genomics in gene
prediction. Functional
Genomics &
Comparative
Genomics will be
discussed
V. Students will learn the Chalk & board method and Assignments and Class
various approaches for Powerpoint presentations. presentations with hands
protein tertiary Group discussions will be on computer training.
structure prediction, held. Students will be assigned
tools used and the task of identifying
validation methods tools used in structure
employed. based drug discovery from
research papers.
4. Keywords
Biological Databases, NCBI, PDB, Visualization Softwares, Sequence Alignment,

BLAST, Gene Prediction, Secondary Structure Prediction, Protein Structure Prediction.
139
Microbial Techniques (BCH SEC-5)
Semester - IV
This course aims to impart basic understanding of microbial techniques by hands-on-

experience on working with microorganisms. It will also provide knowledge about various
control methods for the growth of microbes and the characteristic features of different microbes
After completion of this course, a student will be able:
 To visualize and identify various microorganisms

 To culture microorganisms in aseptic conditions
 To prepare and sterilize different types of media
 To maintain different types of cultures
 To carry out research using microorganisms.
 To learn the principles behind and importance of sterilization while working in varied
areas of biology in various laboratories.
2.2 Course Contents
THEORY
UNIT I: Introduction No. of hours: 4
Development of microbiology as a discipline, Spontaneous generation vs. biogenesis.

Contributions of Anton von Leeuwenhoek, Louis Pasteur, Robert Koch, Joseph Lister and
Alexander Fleming. Development of various microbiological techniques and golden era of
microbiology.
UNIT II: Microbial nutrition and growth No. of hours: 8
The common nutrient requirements. Nutritional types of microorganisms. Culture media and
its components, Synthetic or defined media, Complex media, Enriched media, Selective media,
Differential media. Isolation of Pure culture: Streaking, Serial dilution and Plating methods,
cultivation, maintenance of pure cultures. Microbial Growth: phases of growth, measurement
of microbial growth
140
UNIT III: Control of microorganisms by physical and chemical methods
No. of hours: 6
Mechanism of Dry Heat, Moist Heat, Hot air oven, Filtration and Radiations, Use of Phenolics,
alcoholics, halogens, heavy metals, aldehydes and gases for sterilization.
UNIT IV: Bacterial, Fungal and Algal cell organization and staining
No. of hours: 8
Overview of characteristic features of bacterial, fungal and algal cell. Composition and detailed
structure of gram- positive and gram- negative cell wall. Simple staining and negative staining
of bacteria. Mechanism of gram staining.
UNIT V: Introduction to Viruses No. of hours: 4
General characteristic features of viruses. Nacked and envelop viruses. Examples of RNA and
DNA viruses. Subviral particles: viroids, prions, virusoids and their importance. Isolation and
cultivation of viruses. Virus purification and assays
PRACTICALS
1. Microbiology Laboratory: Basic rules and requirements.

2. To study the principle and applications of important instruments (biological safety
cabinets, autoclave, incubator, BOD incubator, hot air oven, light microscope, pH
meter) used in the microbiology laboratory.
3. Preparation of glassware for microbiological work, cotton plugs, medium and their
sterilization.
4. Sterilization of heat sensitive material by filtration.
5. Demonstration of presence of microflora in the environment by exposing nutrient agar
plates to air.
6. Study of different shapes of bacteria, fungi and algae using permanent
slides/pictographs
7. To stain bacteria using crystal violet/methylene blue.
8. To perform Gram’s staining.
9. To prepare temporary mount of algae.
10. To prepare temporary mount of fungi.
11. Isolation of pure cultures of bacteria by streaking method.
12. Enumeration of colony forming units (CFU) count by spread plate method/pour plate
13. Study the morphological structures of viruses (DNA and RNA) and their important
characters using electron micrographs.
14. Isolation and enumeration of bacteriophages (PFU) from water sample.
2.3 References
1. Willey, J.M, Sherwood, L.M. and Woolverton, C.J. (2017). Prescott’s Microbiology,
(10th ed.), McGraw Hill Higher Education; ISBN13: 9781259657573.
2. Pelczar, Jr M.J., Chan, E.C.S and Krieg, N.R. (2004). Microbiology, (5th ed.), Tata
McGraw Hill; ISBN13: 9780074623206.
141
3. Cappucino, J. and Sherman, N. (2013). Microbiology: A Laboratory Manual. (10th ed.)
Pearson Education Limited; ISBN13: 9780321840226
1. Madigan, M.T., Martinko, J.M., Dunlap, P.V. and Clark, D.P. (2010). Brock Biology
of Micro-organisms. (13th ed.) Pearson Education, Inc. ISBN 13: 9780321649638.
2. Dubey, R.C. and Maheshwari, D.K. (2010). Practical Microbiology. (1st ed.). S.
Chand. ISBN: 81-219-2153-8.

I. Students will gain Chalk and board teaching Internal assessment tests
overall knowledge method, regular question- (midterm and end-term)
and understand the answer activities. Consultation will be conducted.
significance of of text books and reviews Students will be assigned
microbiology as a various topics and will be
discipline asked to deliver a power-
point presentation on the
assigned topics.
II. Students will gain Students will be asked to Assessment through class
insight into nutrient orally revise the previous class test at the end of the
requirements of before every new class helping module. Questions will be
microbes, microbial them in better understanding of given as a part of the
growth and different the particular topic. Teaching assignment. Students will
types of cultures and will be conducted both through also be assessed on the
media used for the black board mode and basis of their performance
growth of microbes. powerpoint presentation mode. and involvement during
practical classes.
III. Students will learn Students will be asked to Assessment through
about the control of orally revise the previous class interactive discussion in
microorganisms by before every new class helping the class and periodic
various physical and them in better understanding of question-answer sessions
chemical methods. the particular topic. Teaching during teaching.
will be conducted both through
powerpoint presentation mode.
IV Students will learn Students will be asked to Assessment through class
about the bacterial, orally revise the previous class test at the end of the
fungal and algal cell before every new class helping module. Questions will be
organization and them in better understanding of given as a part of the
staining. the particular topic. Teaching assignment.
will be conducted both through
142
V. Students will learn Students will be asked to Students will be evaluated
about general orally revise the previous class through class discussion
characteristics of before every new class helping and their performance and
viruses and subviral them in better understanding of involvement during
particles like viriods,
the particular topic. Teaching practical classes
prions and virusoids.will be conducted both through
4. Keywords
Microorganisms, microbial growth, staining, culture, media
143
Acknowledgements
The following individuals are acknowledged for their help in drafting, editing, revising
and preparing the draft of the revised syllabus:
I. Programme Coordinator and Head : Professor Suman Kundu

(Dean, Faculty of Interdisciplinary Department of Biochemistry
and Applied Sciences) UDSC, New Delhi
II. Course Coordinators and Faculty members
Department of Biochemistry : Professor Vijay K. Chaudhary

UDSC, New Delhi Professor Debi P. Sarkar
Professor Alo Nag
Dr. Amita Gupta
Dr. Garima Khare
III. Working Committee Members (teachers) from Department of Biochemistry of the

following colleges – Daulat Ram College, Deshbandhu College, Institute of Home
Economics, Shivaji College, Shaheed Rajguru College of Applied Sciences for
Women, Sri Venkateswara College, Bhaskaracharya College of Applied Sciences -
Dr. Meenakshi Kuhar, Dr. Rajni Jain, Dr. Sunita Singh, Dr. Nandita Narayanasamy,
Dr. Jayita Thakur, Dr. Bhupinder Kumar, Dr. N. Latha, Dr. Radhika Gupta, Dr.
Meenakshi Vaccher, Dr. Renu Baweja, Dr. Prabha Arya, Dr. Padmshree Mudgal, Dr.
Archana Burman, Dr. Sarita Nanda, Dr. Nitika Kaushal, Dr. Shalini Sen, Dr. Nalini M.
Wali, Dr. Radhika Gupta, Dr. Nimisha Sinha, Dr. Vanshika Lumb, Dr. Rashmi
Wardhan, Dr. Vandana Malhotra, Dr. Taruna Arora, Dr. Neena R. Wadehra, Dr.
Sadhna Jain, Dr. Leena Vig, Dr. Ravindra Verma, Dr. Anita Mangla, Dr. Anita Sondhi,
Dr. Darshan Malik, Dr. Anita Goel, Dr. Sarika Yadav, Dr. Kameshwar Sharma, Dr.
Neeraj Dohare, Dr. Neeru Dhamija, Dr. Preeti Karwal, Dr. Anju Kaicker, Dr. Kamna
Singh
IV. Working Committee Student Members from Department of Biochemistry –
Ms Meenakshi Tyagi, Ms Simran Motwani (several of their colleagues also participated)
The following individuals / statutory bodies provided suggestions, critical feedback and
intellectual input –
I. Committee of Courses, Department of Biochemistry – Professor Suman Kundu,

Professor Vijay K. Chaudhary, Professor Debi P. Sarkar, Professor Alo Nag, Professor
Rani Gupta (Expert and external member), Professor Indranil Dasgupta (Expert and
external member), Dr. Amita Gupta, Dr. Garima Khare, Dr. Sarita Nanda (College
Representative), Ms Nupur (Ph.D. student), Ms Nidhi Mittal (M.Sc. Final), Mr. Pranshu
Kothari (M.Sc. Previous), Dr. Meenakshi Kuhar (Special Invitee), Dr. Archana Burman
(Special Invitee)
144
II. Faculty members, Faculty of Interdisciplinary and Applied Sciences – This body consists
of about 55 members including faculties of all the eight departments under FIAS as per
guidelines for constitution of committee, teachers from colleges and external experts
(Professor Sudhir Sopory, Ex-Vice Chancellor, JNU and Scientist, ICGEB; Professor
Rajiv Bhat, JNU; Professor R.N.K. Bamezai, JNU; Dr. Rajesh Gokhale, NII; Professor
S.K. Kaul, IIT, Delhi).
III. International Experts – (i) Professor Guru Rao, Associate Vice President for Research
& Research Integrity Officer and Professor, Roy J. Carver, Department of Biochemistry,
Biophysics and Molecular Biology, Iowa State University, Ames, USA, (ii) Professor
Pradip Raychaudhari, Professor of Department of Biochemistry and Molecular Genetics,
College of Medicine at Chicago, The University of Illinois at Chicago, USA.
IV. National Experts - (i) Professor R.S. Dubey, Department of Biochemistry, Institute of
Science, Banaras Hindu University, Varanasi and former Vice Chancellor, Tilka Manjhi
Bhagalpur University and Guru Ghasidas University and Chairperson, LOCF Task Force
for Biochemistry undergraduate course; (ii) Professor Subrata Sinha, Professor and Head
of Biochemistry, All India Institute of Medical Sciences, New Delhi and former Director,
National Brain Research Centre, Gurugram; (iii) Professor Chandi C. Mandal, Professor
and Head, Department of Biochemistry, School of Life Sciences, Central University of
Rajasthan; (iv) Professor Satheesh Raghavan, Professor of Biochemistry, Indian Institute
of Science (IISc.), Banguluru; (v) Professor Pradeep Burma, Professor of Genetics,
University of Delhi South Campus.
V. Industry expert - Dr. Anil G. Bhansali, Sai Phytoceuticals Pvt. Ltd., New Delhi
VI. Principals of DU Colleges - (i) Dr. Hemlatha Reddy, Sri Venkateswara College; (ii) Dr.
Geeta Trilok-Kumar, Director, Institute of Home Economics; (iii) Dr. Shashi Nijhawan,
Shivaji College.
VII. Teachers of Department of Biochemistry of the various colleges listed above.
VIII. Alumni of the department – Dr. Manish Shandilya (Assistant Professor, Amity,
Gurugram); Dr. Richa Arya (Post-doc Associate, USA); Ms Mehak Zahoor Khan (Ph.D.
student, NII, New Delhi); Dr. Vaibhav Chand (Post-doctoral Research Associate, USA);
Mr. Vaibhav Kumar Nain (Ph.D. Student, THSTI, India); Dr. Kanika Saxena (Post-
doctoral Fellow, Sweden); Dr Chitvan Mittal (Post-doc Associate, USA)
IX. Feedback from stakeholders and well-wishers received through LOCF team, University
of Delhi.
145

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दिल्ली दिश्िदिद्यालय

(Effective from Academic Year 2019-20)

Revised Syllabus as approved by

Applicable for students registered with Regular Colleges, Non Collegiate

Choice Based Credit System (CBCS)

1st Meeting of Teachers / Faculties (13th Feb 2019)

(Syllabus applicable for students seeking admission in the B.Sc.

2. Learning Outcome-based Curriculum Framework in Programme

3. Graduate Attributes in B.Sc. (Hons) Biochemistry 9

4. Qualification Descriptors for Graduates B.Sc. (Hons) Biochemistry 10

5. Programme Learning Outcomes for in B.Sc. (Hons) Biochemistry 10

6. Structure of in B.Sc. (Hons) Biochemistry 13

7. Courses for Programme B.Sc. (Hons) Biochemistry 19-143

For multi-faceted development of a student, the curriculum includes courses to gain

Two value-based courses (Ability Enhancement Compulsory Courses - AECC) in the

1a. Nature and Extent of the B.Sc. (Honours) Programme in Biochemistry

1b. Aims of the Programme

The program aims to:

1c. Program Duration, Design and Structure

Structure of the Programme:

Six courses of Discipline-Specific Electives (DSE) are offered in the programme, of

2. Learning Outcome-based Approach to Curriculum Planning

3. Characteristic Attributes of a Graduate in Biochemistry

 Disciplinary knowledge and skills: Capable of demonstrating (i) comprehensive

 A student should demonstrate (i) a comprehensive and coherent understanding of the

5. Programme Learning Outcomes (PO)

PO1: Inculcate the basic concepts of biochemistry including an understanding of the

Method Description Direct or

Discipline Specific Elective (Any four)

BCH DSE-1: Nutritional Biochemistry

Generic Elective (Any four)

BCH GE-1: Biomolecules

Ability Enhancement Compulsory Course

Skill Enhancement Elective Course (Any two)

BCH SEC-1: Biochemical Techniques

SEMESTER COURSES OFFERED COURSE NAME CREDITS

2.1 Course Learning Outcomes

On successful completion of the course students will be:

2.2 Course Contents

CREDITS: 4 TOTAL HOURS: 60

UNIT I : The foundations of biochemistry No. of hours : 6

UNIT II: Amino Acids No. of hours : 8

Structural features and classification; Physical properties, optical properties

UNIT III: Carbohydrates and Glycobiology No. of hours : 16

Monosaccharides - structure of aldoses and ketoses; Ring structure of sugars, conformations of

UNIT IV: Lipids No. of hours : 14

UNIT V: Nucleic Acids No. of hours : 10

Unit VI: Vitamins No. of hours : 6

CREDITS: 2 TOTAL HOURS: 60

1. Safety measures in laboratories.

Facilitating the Achievement of Course Learning Outcomes**

Unit Course Learning Teaching and Learning Assessment Tasks

Carbohydrates; Lipids; Nucleic acids; Amino acids; Vitamins; Water; Buffers

2.1 Course Learning Outcomes

 Learn about cell theory and basic cell structure

CREDITS: 4 TOTAL HOURS: 60

UNIT I: Introduction to Cell Biology No. of hours: 5

UNIT II: Tools of Cell Biology No. of hours: 10

Cell Fractionation techniques: Principle of centrifugation, Sedimentation Coefficient,

UNIT III: Cell Organelles (structure and function) No. of hours: 17