Chemistry 1 11 Q2 M16

Download as pdf or txt
Download as pdf or txt
You are on page 1of 12

General

Chemistry 1 11
General Chemistry 1 – Grade 11
Quarter 2 – Module 16: The Formation, Structure and Properties of Polymers of
Proteins
First Edition, 2020

Republic Act 8293, section 176 states that: No copyright shall subsist in
any work of the Government of the Philippines. However, prior approval of the
government agency or office wherein the work is created shall be necessary for
exploitation of such work for profit. Such agency or office may, among other things,
impose as a condition the payment of royalties.

Borrowed materials (i.e., songs, stories, poems, pictures, photos, brand


names, trademarks, etc.) included in this module are owned by their respective
copyright holders. Every effort has been exerted to locate and seek permission to use
these materials from their respective copyright owners. The publisher and authors
do not represent nor claim ownership over them.

Published by the Department of Education Division of Pasig City

Development Team of the Self-Learning Module

Writer: Ginalyn P. Bramaje


Editor: Ma. Victoria G. Señase
Reviewer: Ma. Victoria G. Señase
Technical: Emmanuel B. Penetrante
Illustrator: Edison P. Clet
Layout Artist: Mark Kihm G. Lara
Management Team: Ma. Evalou Concepcion A. Agustin
OIC-Schools Division Superintendent
Aurelio G. Alfonso EdD
OIC-Assistant Schools Division Superintendent
Victor M. Javeña EdD
Chief, School Governance and Operations Division and
OIC-Chief, Curriculum Implementation Division

Education Program Supervisors

Librada L. Agon EdD (EPP/TLE/TVL/TVE)


Liza A. Alvarez (Science/STEM/SSP)
Bernard R. Balitao (AP/HUMSS)
Joselito E. Calios (English/SPFL/GAS)
Norlyn D. Conde EdD (MAPEH/SPA/SPS/HOPE/A&D/Sports)
Wilma Q. Del Rosario (LRMS/ADM)
Ma. Teresita E. Herrera EdD (Filipino/GAS/Piling Larang)
Perlita M. Ignacio PhD (EsP)
Dulce O. Santos PhD (Kindergarten/MTB-MLE)
Teresita P. Tagulao EdD (Mathematics/ABM)

Printed in the Philippines by Department of Education – Schools Division of


Pasig City
General
Chemistry 1 11
Quarter 2
Self-Learning Module 16
The Formation, Structure and Properties of
Polymers of Proteins
Introductory Message
For the facilitator:

Welcome to the Chemistry 1 Self-Learning Module 16 on The Formation,


Structure and Properties of Polymers of Proteins

This Self-Learning Module was collaboratively designed, developed and


reviewed by educators from the Schools Division Office of Pasig City headed by its
Officer-in-Charge Schools Division Superintendent, Ma. Evalou Concepcion A.
Agustin, in partnership with the City Government of Pasig through its mayor,
Honorable Victor Ma. Regis N. Sotto. The writers utilized the standards set by the K
to 12 Curriculum using the Most Essential Learning Competencies (MELC) in
developing this instructional resource.

This learning material hopes to engage the learners in guided and independent
learning activities at their own pace and time. Further, this also aims to help learners
acquire the needed 21st century skills especially the 5 Cs, namely: Communication,
Collaboration, Creativity, Critical Thinking, and Character while taking into
consideration their needs and circumstances.

In addition to the material in the main text, you will also see this box in the
body of the module:

Notes to the Teacher


This contains helpful tips or strategies that
will help you in guiding the learners.

As a facilitator you are expected to orient the learners on how to use this
module. You also need to keep track of the learners' progress while allowing them to
manage their own learning. Moreover, you are expected to encourage and assist the
learners as they do the tasks included in the module.
For the Learner:

Welcome to the Chemistry 1 Self-Learning Module 16 on The Formation,


Structure and Properties of Polymers of Proteins

This module was designed to provide you with fun and meaningful
opportunities for guided and independent learning at your own pace and time. You
will be enabled to process the contents of the learning material while being an active
learner.

This module has the following parts and corresponding icons:

Expectations - This points to the set of knowledge and skills


that you will learn after completing the module.

Pretest - This measures your prior knowledge about the lesson


at hand.

Recap - This part of the module provides a review of concepts


and skills that you already know about a previous lesson.

Lesson - This section discusses the topic in the module.

Activities - This is a set of activities that you need to perform.

Wrap-Up - This section summarizes the concepts and


application of the lesson.

Valuing - This part integrates a desirable moral value in the


lesson.

Posttest – This measures how much you have learned from the
EXPECTATIONS
This module is about the formation, structure and properties of polymers of
carbohydrates. After going through this module, you are expected to:

• describe the formation, structure and properties of polymers of proteins


and relate them to their function;
• demonstrate an understanding about the polymers of proteins;
• recognize the importance of proteins in man’s life.

PRETEST

Let’s try to answer this! Choose the letter of the best answer.

1. What do you call the repeating units of protein?


A. amino acids C. glucose units
B. fatty acids D. peptides
2. Which is the feature of the primary structure of protein?
A. Subunit structure of protein
B. Helical structure of protein
C. 3 dimentional structure of protein
D. Linear sequence of amino acids joined by peptide bond
3. A How does the tertiary structure of a protein differ from the secondary
structure?
A. The tertiary structure has a 3D shape, while the secondary structure is
often folded or pleated.
B. The tertiary structure is made of two or more polypeptides, while the
secondary structure is made form only one polypeptide.
C. The tertiary structure is pleated into an alpha helix, while the secondary
structure is completely linear.
D. The tertiary structure is a sequence of amino acids, while the secondary
structure contains several polypeptides.
4. Which is NOT a function of proteins?
A. serve as the primary energy source
B. make up body structures
C. act as hormones
D. act as enzymes
5. The major protein component of human hair is α-keratin. Hair ‘straighteners’
are commonly used tools which use heat to iron hair into temporarily lying
flat and straight. What is the best biological explanation for this phenomenon?
A. Hair straighteners disrupt ionic bonds between -keratin molecules.
B. Hair straighteners denature protein by disrupting the pH.
C. Hair straighteners disrupt hydrogen bonds in -keratin
D. Hair straighteners disrupt disulfide bridges in -keratin
RECAP

Lipids are also recognized as a major player in human health issues. Thus, it
is necessary to watch for the lipid profile of an individual to avoid health problem.
In addition, there are different classes of Lipids. Can you identify the classes of
lipids given below?

1. Fats/oil
2. Phospholipids
3. Cholesterol
4. Waxes
5. Vitamins A,D,E,K

God job! Your retention is so good!

LESSON

Have you ever think which is responsible for your curly or straight hair, the
keratin of your skin and fingernails, the insulin that regulates glucose metabolism
in the body and the DNA polymerase that catalyzes the synthesis of DNA in cells?

It sounds interesting right? Do you know that proteins are responsible for all
the listed functions? Yes! Proteins are large biomolecules that found in every living
organism. They are of many types and have a lot of biological functions.

What are proteins made of ?


Proteins are made up of many amino acid units linked together by amide
bonds in a long chain. Below is the structure of amino acid.

Have you observed the two functional groups of amino acids? What are they?
A. Basic amino group (NH2)
B. Acidic carboxyl group (COOH)
Amino acid serves as the building blocks for proteins stems. And there are 20
kinds of amino acids depending on their R-group. The simplest amino acid is glycine
where R is a hydrogen atom. The chain of amino acids linked together with fewer
than 50 are usually called peptides. Thus, when many amino acids are linked
together through peptide bonds, this molecule is known as polypeptide. When a
very large number of amino acids are linked together it results in a protein.

Classes of Proteins

Proteins

Simple Conjugated Derived


Proteins Proteins Proteins

Figure 1. Classes of Proteins

1. Simple Proteins- yield only amino acids and no other compounds on hydrolysis.

A. Fibrous Proteins- consist of polypeptide chains arrange side by side in long


filaments and insoluble in water. Examples: keratin in nails and hair, collagen
in muscle
B. Globular Proteins-nearly circular shapes, which normally coiled into compact.
They are soluble in water. Examples: hemoglobin from blood, insulin, enzyme

2. Conjugated Proteins-yield other compounds in addition to amino acids on


hydrolysis. It is more common than simple proteins.

3. Derived Proteins-They are formed from large molecular weight proteins by the
action of heat, enzymes or chemical agents, thus they have lower molecular
weights. They are derivatives or degraded products of simple and conjugated
proteins. They may be :
a. Primary derived protein: Proteans, Metaproteins, Coagulated proteins
b. Secondary derived proteins: Proteosesn or albunoses, peptones,
peptides.

Different Levels of Protein Structure

The different functions of proteins are dependent on the sequence and


structure of proteins. Thus, there are different levels of Protein Structure:
1. Primary Structure-it is the sequence of amino acids which is linear and
linked together by peptide bonds. It is the most fundamental structural level.
2. Secondary Structure- in this level the polypeptide chain can twist and fold
in different ways because single bonds in the polypeptide chain allow rotation.
3. Tertiary structure- in this level the entire protein molecules coils into an
overall three dimensional shape.

4. Quaternary Structure- in this level several protein molecules join together to


form a bigger cluster structure.

https://www.google.com/search?q=different+level+of+structure+of+proteins&rlz
1C1CHBD_enPH825PH913&source=lnms&tbm=isch&sa=X&ved=2ahUKEwiDgIJhIbrAh
WFQN4KHeqGDPgQAUoAXoECA0QAw&biw=1366&bih=657#imgrc=3J52drLFpk6_YM

Property of Protein

1. Denaturation. A partial or complete unfolding of the natural conformation of


the polypeptide chain. This is caused by heat, acids, alkalies, alcohol,
acetone, urea, beta- mercaptoethanol.
2. Coagulation. Insoluble aggregates called coagulum are formed when proteins
are denatured by heat. There are few proteins like albumins, globulins are
heat coagulable.
3. Isoelectric pH. A pH in which the negative and positive charges has equal
number.
4. Molecular Weights of Proteins. Different proteins have different amino acid
composition and hence their molecular weights differ. The molecular weights
of proteins range from 5000 to 10 9 Daltons

Functions of Proteins

Proteins functions are endless and are essential for the growth and repair.
They also have broad diversity of biological function and are the most significant final
products of the information pathways. Here are some of the biological functions of
proteins:
1. They act as biological catalyst (enzyme) such as chymotrypsin.
2. They act as the defense against infections by means of protein antibodies.
3. They are responsible in the transport of oxygen and carbon dioxide by
hemoglobin and special enzymes in the red cells.
4. They serve as structural components such as keratin of hair and nail, collagen
of bone etc.
5. They act as hormone that regulate body processes such as insulin.
6. They serve as the storage of nutrients such as casein.
7. They are involved in blood clotting through thrombin, fibrinogen and other
protein factors.

ACTIVITIES

ACTIVITY 1: “Protein Facts”


Direction: Answer the questions below.

1. What elements (atoms) are proteins made of?


2. Unlike carbohydrates and lipids, proteins contain which element?
3. What types of food can you find proteins in ?
4. What is the monomer of a protein?
5. What part an amino acid’s chemistry determines the function of a protein?
6. How many different common amino acids are there?
7. What type of catalyst is made of proteins?
8. What organic compound is made of proteins and help fight disease?

ACTIVITY 2: “The Hierarchy of Protein Structure”


Study and analyze the level of Protein Structure, and answer the guide questions
below.

1.Which structure of a protein consists of a linear sequence of amino acids?


2. Which protein structure gives the protein its actual function?
3. Which protein structure has coiled regions folded into a 3-D shape?
4. Which protein structure has two or more polypeptides bound to each other ?
5. Which protein structure has two possible helices?
ACTIVITY 3: “Nutrition Question Card”
Direction: Proteins have different functions in our body. Answer the nutrition card
in the boxes below.

Protein Protein
If I don’t eat enough protein this could Name three protein rich foods.
happen...
a. nails fall off
b. you lose your balance and fall
c. hair falls off, teeth will rot

Protein Fats
What does protein do for you? What food group causes the calories to
a. changes your hair color triple in
b. helps you grow chicken if it is fried?
c. makes you popular in school
d. allows you to eat more candy

WRAP-UP
Let’s take a closer look at the chemistry of protein. Fill in the blanks.

Proteins are natural polymers. They are made from the linkage of monomers called
(1)____________________. Amino acids have two functional groups; namely,
(2)________________ and (3)_______________. The bond that links amino acids together
is known as (4)______________. There are different level of protein structure namely:
(5)______________, ________________,_____________,_____________. There are important
functions of proteins, such as ___________________________.

Finally, you made it! Take your last step and good luck!
VALUING
The Power of Protein
Protein is an essential component of every cell in the body. And, it is an
important building block of bones, muscles, cartilage, skin, and blood. Thus,
everyone needs a right amount of protein intake which come from the food we eat.
Like what they always remind us “health is wealth”. So, as an individual how can
you make yourself healthy and physically fit?

POSTTEST

Direction: Choose the letter of the best answer.

1.Which part of the amino acid gives it uniqueness?


A. Amino group C. Side chain
B. Carboxyl group D. None of the mentioned
2. Which of the following information is responsible to specify the three-
dimensional shape of a protein?
A. The protein’s peptide bond
B. The protein’s amino acid sequence
C. The protein’s interaction with other polypeptides
D. The protein’s interaction with molecular chaperons
3. During the formation of the peptide bond which of the following takes place?
A. Hydroxyl group is lost from its carboxyl group of one amino acid and a
hydrogen atom is lost from its amino group of another amino acid
B. Hydrogen atom is lost from its carboxyl group of one amino acid and a
hydroxyl group is lost from its amino group of another amino acid
C. Hydroxyl group is lost from its carboxyl group of one amino acid and a
hydroxyl group is lost from its amino group of another amino acid
D. Hydrogen atom is lost from its carboxyl group of one amino acid and a
hydrogen atom is lost from its amino group of another amino acid?
4. The building blocks of proteins are ______ naturally occurring amino acids, small
molecules that contain a free amino group (NH2) and a free carboxyl group (COOH).
A. nine C. ten
B. nineteen D. twenty
5. Mother of a malnourished child has been instructed to include a complete protein
in diet for her child, which out of the followings proteins should be recommended?
A. Milk C. Pulses
B. Soy Protein D. Wheat

You might also like