MPSTME (2019-20)

Elements of Biology

MODULE 1- INTRODUCTION
Science and Engineering
Science is about knowing and engineering is about doing. Science is synthesis of
knowledge by understanding the law of nature, while engineering is the application of
knowledge to transform the nature for serving people. Engineers use the scientific knowledge
to build processes, structures and equipment. Both engineers and scientists have sound
knowledge of science, mathematics and technology, but engineers are trained to use these
principles in designing creative solutions to the challenges. Science is about studying what is
existing, engineering is about creating what never was. Science and engineering, both
complement each other, for to transform nature effectively requires proper understanding, and
to discover nature’s secrets requires instruments to modify it in experiments.

Scientist-engineer and science-engineering can be considered to be two perpendicular axes in

a two-dimensional space. Then, the actions of scientists and engineers involved in a project can
be plotted as points in the plane defined by these axes.
Engineers applied the knowledge of avian adaptations of flying to develop aircraft. The
fundamentals of aircraft is similar to that of a bird. Aircrafts were designed in the shape of a
bird. As the birds position their legs close to the body while taking off and flying, similarly
wheels of the airplane hide inside the body after taking off and lowered during landing.
Airplane use their wings to change the direction like birds.
The study of human eye by biologists was used in the development of camera. The
photographic camera resembles the human eye. The shutter acts as the eye lids, iris as the
diaphragm, aperture acts as the pupil, the camera lens is similar to the eye lens and the light
sensitive film resembles the retina. In both the cases, the image formed is small and inverted.
Importance of Biology
Biology comprises the area of study that focus on life at a variety of levels and from a
diversity of perspectives. It covers the areas such as the transfer of hereditary material from
organism to organism, the relationship between diet and disease, and the development of new
food plants. The exploration of biology advances knowledge in applied fields such as medicine,
agriculture, and industry and results in the creation of products that enhance and lengthen lives.
As a result of observing living things, their environments, and the interactions between them,

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 MPSTME (2019-20)
Elements of Biology
biologists have posed questions; put forth hypothesis based on their observations, and tested
their predictions of the living world. Rising out of this abundance of tested predictions are the
themes, or accepted explanations of life that permeate the science of biology. Organisms in an
ecological system have different forms, sizes, and linkages with each other, and also with vastly
different forms. The simplest form of life is exhibited by certain macromolecular forms
encapsulated in a protein coat, which are the sub-microscopic DNA and RNA viruses. Living
being exhibit growth. It is not a defining property of living organisms, but is a characteristic
and depends upon various factors such as reproduction.
Applications of Biology
All sciences, including biology, are a way of understanding the world. Studying biology
involves learning about problem solving, the way scientists go about their work, and worlds
you may know little about, like the world of microbes. Studying biology involves learning how
to protect the planet and how to take care of your body Molecular biology plays an important
role in controlling processes from production to sale of food and protecting the health of
consumers. In agriculture, various modern biological methods are used for crop production and
to kill harmful insects. Biology has made a lot of progress to understand the causes of many
diseases, methods of controlling, curing disease, and formulating drugs. Several industries like
fishing, pearl, silk etc., have developed by adopting new technologies received from knowledge
of biology. Biotechnology can be stated as any technological application employing biological
systems or living organisms to synthesize or modify some products or processes for specific
use. Biotechnology is also the science dealing with the industrial scale production of
pharmaceuticals and biological compounds using genetically modified organisms such as
plants, animals, fungi, bacteria etc.
Brownian Motion
This pattern of motion typically alternates random fluctuations in a particle's position
inside a fluid sub-domain with a relocation to another sub-domain. Each relocation is followed
by more fluctuations within the new closed volume. This pattern describes a fluid at thermal
equilibrium, defined by a given temperature. Within such fluid there exists no preferential
direction of flow as in transport phenomena. More specifically the fluid's
overall linear and angular momenta remain null over time. It is important also to note that
the kinetic energies of the molecular Brownian motions, together with those of molecular
rotations and vibrations sum up to the caloric component of a fluid's internal energy.
This motion is named after the botanist Robert Brown, who was the most eminent
microscopist of his time. In 1827, while looking through a microscope at pollen of the
plant Clarkia pulchella immersed in water, the triangular shaped pollen burst at the corners,
emitting particles which he noted jiggled around in the water in random fashion. He was not
able to determine the mechanisms that caused this motion. Atoms and molecules had long been
theorized as the constituents of matter, and Albert Einstein published a paper in 1905 that
explained in precise detail how the motion that Brown had observed was a result of the pollen
being moved by individual water molecules, making one of his first big contributions to
science. This explanation of Brownian motion served as convincing evidence that atoms and
molecules exist, and was further verified experimentally by Jean Perrin in 1908. Perrin was

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Elements of Biology
awarded the Nobel Prize in Physics in 1926 "for his work on the discontinuous structure of
matter". The direction of the force of atomic bombardment is constantly changing, and at
different times the particle is hit more on one side than another, leading to the seemingly
random nature of the motion.
The many-body interactions that yield the Brownian pattern cannot be solved by a
model accounting for every involved molecule. In consequence only probabilistic models
applied to molecular populations can be employed to describe it. Two such models of
the statistical mechanics, due to Einstein and Smoluchowski are presented below. Another,
pure probabilistic class of models is the class of the stochastic process models. There exist both
simpler and more complicated stochastic processes which in extreme may describe the
Brownian motion.
Origin of Thermodynamics
The German surgeon Julius Robert von Mayer (1814-1878) started a study on the
physical side of the symptoms of life during his journey in Dutch East India in 1840 and noticed
that the venous blood of the sailors in the tropics is much darker than in cold climates. He
concluded that the chemical processes of the body get their sources of energy for oxidation
from the nature.
Arriving home he wrote a scientific paper in 1841 under the name of Über die
quantitative und qualitative Bestimmung der Kräfte (On the Quantitative and Qualitative
Determination of Forces). It was ignored by the physicists because of its strange argumentation
that were based on the principle of causa aequat effectum so he could publish it next year in a
chemical journal under the title of Bemerkungen über die Kräfte der unbelebten Natur
(Remarks on the Forces of Inorganic Nature). This fundamental paper contained the first
adequate formulation about the Law of Conservation of Energy that although work and heat
are different forms of energy, they can be transformed into one another. He also specified
theoretically the numerical value of the mechanical equivalent of heat as 365mkp (3580J) which
is a little bit far from the real value but the order of size and the deduction was correct. Mayer
also gave suggestions how to transform experimentally kinetic energy into heat.

Tutorial
1. Write a short note on relation between science and engineering. Explain with examples.
2. Write a detailed note on the importance of biology
3. Write a note on applications of biology.
4. Explain with some examples how biological observations of 18th century have lead to major
discoveries.
5. Write a note on the fundamental importance of Brownian motion referring to the original
observation of Robert Brown.
6. Write a note on the origin of thermodynamics referring to the original observation of Julius
Mayer.

***

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1. Your Cornea behaves much like the front lens element of a
lens. Together with the lens, which is behind the iris, they are
the eye’s focusing elements. The cornea takes widely diverging
rays of light and bends them through the pupil, the round
opening in the central portion of the coloured iris.

2. Your Iris and pupil act like the aperture of a camera. The iris
is a muscle which, when contracted, covers all but a small
central portion of the lens, allows adjustable control of the
quantity of light entering the eye so that the eye can work well
in a wide range of viewing conditions, from dim to very bright
light.

3. Finally, your Retina is the sensory layer that lines the very
back of our eyes. It acts very much like the imaging sensor chip
in a digital camera. The retina has numerous photoreceptor
nerve cells that help change the light rays into electrical
impulses and send them through the optic nerve to the brain
where an image (of what we see) is finally received and
perceived. Because of this reception and perception function,
retina is, perhaps, the most important component of our eyes.
As with the camera, if the “film” is bad in the eye (i.e. the
retina), no matter how good rest of the eye is, we will not get a
good quality image or picture.
 No. 722:
JULIUS ROBERT MAYER

by John H. Lienhard

Click here for audio of Episode 722.

Today, a story about blood and heat. The University of Houston's College of
Engineering presents this series about the machines that make our civilization run, and
the people whose ingenuity created them.

In 1840, Robert Mayer was 26. That year he shipped to the East Indies as the surgeon
on a Dutch vessel. Afterward, he came back to Germany, married, and settled down as
a town doctor. It might seem he was done with adventure.

But something touched him in Java, and it changed his life. Whether or not it changed
history is moot. But insight came on Mayer in 1840, and science historians still talk
about it.

He was letting blood from sick sailors. You do that by lancing a vein. Venous blood
carries less oxygen than arterial blood. It runs darker. The first time Mayer opened a
vein in Djarkata, blood ran far too red. He thought he'd hit an artery.

Then he found that's normal in the tropics. And he realized: People burn less of the
food they eat. They generate less heat.

We knew that food fuels our power output. Now Mayer realized that it also fuels our
heat supply. And we need a lot less heat in Djakarta than we do in Europe.

In 1840 we didn't know that heat and work can be traded back and forth. Mayer
thought about that red blood on the long trip back. And he tumbled to the truth of
energy conservation.

Mayer identified our most important physical law. But he didn't know classical
physics. He didn't know formal math. He wrote a clumsy paper about the idea, and the
editor ignored it.

So Mayer went back to study physics. Then he wrote a better paper in 1842.
Meanwhile, a young Englishman, James Joule, was measuring how many foot-pounds
of work made a Btu. By 1847, Joule had honed his accuracy to 99 percent.
And there the plot thickens. Mayer had spun a correct theory for the number of foot-
pounds per Btu. But no one would believe it until measurements were more complete.

Physicists sorted through Mayer's theory and Joule's experiment. When they finally
resolved the whole business, they overlooked Mayer. By 1850 Mayer was angry and
frustrated. He attempted suicide. For years after, he was in and out of asylums.

Finally, in 1863, the Englishman John Tyndall wrote an important text: Heat: A Mode
of Motion. It began and ended with Mayer. Mayer was vindicated.

Twenty years before, insight had touched him in Java. His vision of bright blood and
heat really did change history. But first, professional scientists -- men untouched by
visions -- had to put it in familiar terms. In the meantime, Mayer's insight had almost
driven him mad. And I hear words by the poet Rilke:

. . . if you set this brain of mine on fire,

then on my blood I yet will carry you.
I'm John Lienhard, at the University of Houston, where we're interested in the way
inventive minds work.
(Theme music)
Biomolecules
One of the most mind-boggling facts is that all living things are essentially made up of
non-living atoms and molecules. In chemistry, we strive to learn more about these
molecules that are named biomolecule. Our bodies are made up of various of these
complex biomolecules such as proteins, carbohydrates etc. Let us learn all of these in
some detail

• Carbohydrates
• Structure of Proteins
• Amino Acids
• Enzymes
• Nucleic Acids
• Structure of Nucleic Acids

Carbohydrates
The term carbohydrate is itself a combination of the “hydrates of
carbon”. They are also known as “Saccharides” which is a derivation
of the Greek word “Sakcharon” meaning sugar. The definition of
carbohydrates in chemistry is as follows:

“Optically active polyhydroxy aldehydes or polyhydroxy ketones or

substances which give these on hydrolysis are termed as
carbohydrates”.

Some of the most common carbohydrates that we come across in our

daily lives are in form of sugars. These sugars can be in form of
Glucose, Sucrose, Fructose, Cellulose, Maltose etc.
The general formula for carbohydrate is Cx(H2O)y. Although, it must be
remembered that this is just a general formula. There are various
exceptions to this that we will see. Let us take a look at Acetic Acid
which is CH3COOH. Now although this will fit in the general formula
of carbohydrate i.e. Cx(H2O)y, we know that acetic acid is not a
carbohydrate.

Formaldehyde (HCHO) also falls under this category of this general

formula but is also not a carbohydrate. And on the other hand,
Rhamnose (C6H12O6) which is very much a carbohydrate but does not
follow the general formula.

Classification of Carbohydrates

The main classification of carbohydrate is done on the basis of

hydrolysis. This classification is as follow:

1. Monosaccharides: These are the simplest form of carbohydrate that

cannot be hydrolyzed any further. They have the general formula of
(CH2O)n. Some common examples are glucose, Ribose etc.
2. Oligosaccharides: Carbohydrates that on hydrolysis yield two to ten
smaller units or monosaccharides are oligosaccharides. They are a
large category and further divides into various subcategories.
3. Disaccharides: A further classification of oligosaccharides, these give
two units of the same or different monosaccharides on hydrolysis. For
example, sucrose on hydrolysis gives one molecule of glucose and
fructose each. Whereas maltose on hydrolysis gives two molecules of
only glucose,
4. Trisaccharides: Carbohydrates that on hydrolysis gives three
molecules of monosaccharides, whether same or different. An
example is Raffinose.
5.Tetrasaccharides: And as the name suggests this carbohydrate on
hydrolysis give four molecules of monosaccharides. Stachyose is an
example.

5. Polysaccharides: The final category of carbohydrates. These give a

large number of monosaccharides when they undergo hydrolysis,
These carbohydrates are not sweet in taste and are also known as non-
sugars. Some common examples are starch, glycogen etc.

Importance of Carbohydrates
Now as we previously discussed, carbohydrates are absolutely essential
for life on the planet. Let us take a more detailed look at the importance
of carbohydrates.

• Carbohydrates are responsible for storing chemical energy in living

organisms. You must hear all the time when athletes carbo-load
before a game. This is so they can provide themselves with extra
energy. They are also an important constituent for supporting tissues
in plants and even in some animals.
• As I am sure you are already aware of photosynthesis. It is the
process by which plants utilize solar energy to generate energy for
themselves and food for us. Through this process, plants fix CO2 and
synthesize carbohydrate. Let us take a look at the chemical reaction
occurring during photosynthesis.
x(CO2) + y(H2O) + Solar energy ⇒ Cx (H2O)y + O2

• So carbohydrates due to photosynthesis are the repository of solar

energy in plants, Then when plants or animals metabolize the said
carbohydrate this energy releases. The metabolizing equation is just
the reverse of the photosynthesis equation
Cx (H2O)y + O2 ⇒ x(CO2) + y(H2O) + Energy
Glucose
The most abundant monosaccharide found in nature is in fact glucose. It
is the most abundant organic compound on earth. We can find glucose
in varies fruits, honey and even in starch and cane sugar. We obtain a
large part of the energy in our bodies from glucose through the foods
we eat. It is an aldohexose, which means it has six carbon atoms in its
molecule. Its chemical formula is C6H12O6

We obtain glucose mainly from two sources which are starch and
sucrose. Let us look at how we can prepare glucose from these sources

• On a large and commercial scale glucose is prepared from hydrolysis

of starch by boiling it with dilute H2SO4. The chemical reaction is as
follows
(C6H10O5) + n (H2O) ————-> n ( C6H12O6 )

Starch Glucose

• Also, another way of preparing glucose, with fructose as a joint or by-

product, is to boil sucrose in dilute HCl or even H2SO4 in an
alcoholic solution. This chemical reaction is as follows
C12H22O11 + H2O ————> C6H12O6 + C6H12O6

Sucrose Glucose + Fructose

Fructose
 Fructose is a simple ketonic monosaccharide. We mostly find fructose
in plants and their fruits, flowers and root vegetables, hence earning it a
moniker of fruit sugar. It is also abundantly present in honey and corn
syrup. Generally, fructose bonds with glucose to form a disaccharide we
know as sucrose. Fructose was first discovered by a French chemist
Augustin – Pierre Debrunfaut.

The chemical formula of fructose is also C6H12O6 but the bonding of

fructose is very different than that of glucose. Fructose has a cyclic
structure. The structure is an intramolecular hemiacetal. It has its
carbonyl group at its number two carbon (its a ketone function group).
In its cyclic form, it (generally) forms a five-member ring which we call
a Furanose ring.

Disaccharides
Disaccharides are sugars (carbohydrate molecules) that form when two
simple sugars i.e. monosaccharides combine to form a disaccharide. i.e.
monosaccharides combine to form a disaccharideup of repeating units
of monosaccharides that are attached together by Glucosidic linkage. A
molecule of a polysaccharide has n number of sugar molecules bound
together to form a larger molecule. Another name for them is Glycans.

Polysaccharides are classified into two parts, namely

i. Homopolysaccharide: These molecules are made up of only one type

of monosaccharides. A general theme for them is derived from the
kind of monosaccharide units they have. A homopolysaccharide
made up of only glucose molecules is named Glucans. One with only
galactose molecules earns the name Galactus. In this given topic we
will be focussing only on Glucans.
ii. Heteropolysaccharide: These are polysaccharide molecules
consisting of more than one type of monosaccharides.
Now let us know the three main polysaccharides commonly found in
nature. They are the ones that we see every day in our day to day lives.

1] Starch 2] Glycogen 3] Cellulose

Structure of Proteins
Proteins are what we call biological polymers (i.e. they occur naturally
in nature). Now we previously learnt that amino acids are the building
blocks of proteins. What this actually entails is that proteins are long
chain-like structure, with amino acids being the main ingredient. These
amino acids are connected together with peptide bonds, and a few such
bonds linking together form a polypeptide chain. Now one or more of
these polypeptide chains twist or fold spontaneously and a protein is
formed.

The size of the proteins varies greatly. It actually depends on the

number of polypeptide molecules it contains. One of the smallest
protein molecules is insulin, and the largest being Titin which consist of
34,350 amino acids. Let us now look at the four types of protein
structure that make up a protein molecule.

1] Primary Protein Structure

The primary structure is the unique formation and order in which the
amino acids (the building blocks) combine and link to give us a protein
molecule. Protein gets all its properties from its primary structure.

There are in all twenty amino acids in the human body. All of these
have a carboxyl group and an amino group. But each has a different
variable group known as the “R” group. It is this R group that lends a
particular protein its unique structure.

Every protein is determined by the sequencing of the amino acids. The

formation and ordering of these amino acids in proteins are extremely
specific. If we alter even one amino acid in the chain it results in a non-
functioning protein or what we call a gene mutation.
2] Secondary Protein Structure

After the sequencing of amino acids, we now move on to the secondary

structure. This is when the peptide backbone of the protein structure
will fold onto itself, to give proteins their unique shape. This folding of
the polypeptide chains happens due to the interaction between the
carboxyl groups along with the amine groups of the peptide
chains.There are two kinds of shapes formed in the secondary structure.
These are

• α-helix: The backbone follows a helical structure. The hydrogen

bonds with the oxygen between the different layers of the helix,
giving it this helical structure.
• β-pleated sheet: here the polypeptide chains are stacked next to each
other and their outer hydrogen molecules form intramolecular bonds
to give it this sheet-like structure
3] Tertiary Structures

This is the structure that gives protein the 3-D shape and formation.
After the amino acids form bonds (secondary structure) and shapes like
helices and sheets, the structure can coil or fold at random. This is what
we call the tertiary structure of proteins. If this structure is disrupted or
disturbed a protein is said to be denatured which means it is chemically
affected and its structure is distorted.

4] Quaternary Structure

Finally, we come to the fourth structure. The spatial arrangement of two

or more peptide chains leads to this structure. It is important to note it is
not necessary for proteins to have quaternary structures. Primary,
secondary and tertiary structures are present in all natural proteins, but
the same is not true for quaternary structure. Hence if a protein has only
the first three structures it is considered to be a protein.
Amino Acids
There are some 20 amino acids in the proteins that we consume. These
amino acids bond together to form a larger protein molecule. Amino
acid being organic compound molecules can form various different
links with each other due to the versatile nature of carbon. This enables
the great diversity of proteins that can be found in nature. These are an
essential nutrient in our diet because of the functions they perform.

Structure of Amino Acids

(Source: Wikibooks)

There are actually thousands of amino acids occurring in nature. But

only about 20 amino acids form a part of the proteins in the human
body. These twenty acids will be our focus here. Although all these
have varied structures, the basic structure of amino acid remains
uniform.

All amino acids contain a carbon atom in the middle of the molecule,
the alpha-carbon

• This atom is surrounded by three chemical groups.

• One is an amine group -NH2
• The second one is a carboxyl group -OOOH
 • The third group is denoted by R. This is the variable radical group
and is different for every amino acid. This R group makes the amino
acid unique.
Classification of Amino Acids

Amino Acid can be classified based on their structure and the structure
of their side chains i.e. the R chains. Now two basic subcategories are

1] Non-Polar Amino Acids

These are also known as Hydrophobic. The R group can be either of

Alkyl groups (with an alkyl chain) or Aromatic groups. The acids
falling in this group are stated below. Numbers one to seven are Alkyl
and the last two are aromatic

i. Glycine (H)
ii. Alanine (CH3)
iii. Valine ( CH (CH3)2 )
iv. Methionine ( CH2CH2SCH3 )
v. Leucine ( CH2CH(CH3)2 )
vi. Isoleucine ( -CH(CH3)CH2CH3 )
vii. Proline (special structure)
viii. Phenylalanine
ix. Tryptophan
2] Polar Amino Acids

If the side chains of amino acid contain different polar groups like
amines, alcohols or acids they are polar in nature. These are also known
 as Hydrophilic Acids. These are further divided into three further
categories.

a) Acidic: If the side chain contains an extra element of carboxylic acid

component these are acid-polar amino acids. They tend to donate their
hydrogen atom. These are:

i. Aspartic Acid ( CH2COOH)

ii. Glutamic Acid ( CH2CH2COOH )
b) Basic: These have an extra nitrogen group that tend to attract a
hydrogen atom. The three basic polar amino acids are

i. Histidine
ii. Lysine ( CH2(CH2)2NH2 )
iii. Arginine
c) Neutral: These are neither acidic nor basic. They have an equal
number of amino and carboxyl groups. Also, they have at least one
hydrogen component connected to electronegative atoms. Some of these
neutral acids are

i. Serine ( CH2OH )
ii. Threonine ( CH(OH)CH3 )
iii. Asparagine ( CH2OHNH2 )
Amino acid can also be classified on the basis of their need to the
human body and their availability in the human body
1] Essential Amino Acids

These are the acids that cannot be synthesized in our bodies. We must
rely on food sources to obtain these amino acids. They are

• Leucine
• Isoleucine
• Lysine
2] Non-Essential

These acids are synthesized in our bodies itself and we need not rely on
outside sources for them. They are either produced in our bodies or
obtained from protein breakdowns.

Properties of Amino Acids

Now that we have seen the structure and types of amino acids. Now
from this information, we can arrive at the properties of amino acids.

• Each amino acid has both an acidic and basic group as you can see
from its structure. This is the reason they behave like salts.
• Any amino acid in the dry state is in crystalline form. They exist as a
dipolar ion. The COOH group exists as an anion. And the NH2 group
exists as a cation. This dipolar ion has a special name “Zwitter ions’.
• In aqueous solution, alpha amino acids exist in equilibrium between a
cationic form, an anionic form and dipolar ion.
• The Isoelectric point is the pH point at which the concentration of
zwitter ions is the highest ad the concentration of cationic and anionic
form is equal. This point is definite for every α-amino acid.
• They are generally water soluble and also have high melting points.
Enzyme
Enzymes can be simply described as biological catalysts. Like any
catalyst enables a chemical reaction, they do the same for your body. In
most reaction energy has to be provided, usually in form of heat.
Enzymes actually reduce the activation energy needed and increase the
velocity of biological reactions in the human body. But in this
process/reaction, they do not undergo any changes themselves. Hence
this is the reason they are recyclable and the required in very small
doses.

Structure of an Enzyme

Enzyme is a form of protein. As far as the structure goes they are

globular, that is they are cylindrical in shape. Their polypeptide chains
have a coil-like formation.

The sequencing of the amino acids decides not only define the structure
of an enzyme but also its functions. The distinctive structure of an
enzyme will determine its catalytic activity. In a particular configuration
(or sequencing) a particular portion of the structure, known as the active
site is accessible to attract and catalyze the reactants.
Functions of an Enzyme

Now enzymes are highly specific in their functions. A particular

enzyme will only act as a catalyst for a particular reaction. In a given
specific reaction the molecules that an enzyme reacts with is
a substrate.

The substrate binds itself to the active site of the enzyme. This is the
lock and key theory. So only the correct enzyme can react with the
correct substrate, just like only the perfect key can unlock a particular
lock. Although in modern times we believe that the substrate alters its
binding to fit with the active site, This is known as induced fit.

After the catalyses of the substrate, we are left with what we call the
products. It is important to note that throughout this entire process the
molecular structure of the enzymes does not undergo permanent
alteration. It keeps its structure enact and performs its functions again.

Just like proteins, enzymes can also be denatured. This happens when
their structure changes due to some external force or pressure.
Generally, heat causes them to denature and lose their catalyzing
abilities.
Classification of Enzymes

The classification of an enzyme is on the basis of the reaction they

catalyze. The classification is as follows

• Oxidoreductases: Catalyze oxidation-reduction reactions

• Transferases: These obviously catalyze reactions of group transfer
• Hydrolases: Hydrolysis reactions are catalyzed by them
• Lyases: one of the lesser known enzymes
• Isomerases: These change the shape of the molecule after catalysing
its structural shifts
• Ligases: And these catalyze ligation processes
Nucleic Acid
It can be said that nucleic acid is one of the most important
biopolymers. They are present in all organisms. Think of them as the
mother chip of your body. This is where your genetic information is
encoded and recorded. The function of nucleic acid is to express this
information outside the cell to the future generation. So it felicitates the
transfer of genetic information from one generation to the next and so
onwards.

Now nucleic acids are big and complex molecules. They have a linear
binding between nucleotides. They are double-stranded and have highly
complex sequencing.

Nomenclature

The initial discovery of nucleic acid was through their presence in the
nucleus of eukaryotic cells. Hence the name contains a reference to the
nucleus. Later they were discovered to contain phosphate group like in
phosphoric acid. And the name was now nucleic acids. The name is also
a version of polynucleotide since the structure is linear chains of
nucleotides.

Types of Nucleic Acids

Now there are two main types of nucleic acids, namely
Deoxyribonucleic Acid and Ribonucleic Acid. And although the name
sounds complicated you will be surprised to know you are already
aware of them both. They are nothing but DNA and RNA. Let us study
these both in a little more detail.
Deoxyribonucleic Acid

Better known as DNA this is the first type of nucleic acid. You are
probably aware of DNA and know that every humans DNA is unique to
themselves. But how does this happen and what exactly is DNA.

There are approximately 200 types of cells in our bodies like white
blood cells, neurons (brain cells), cardiac muscle cells etc. But how do
these cells know their particular function? Well, their chemical
compositions within their cells differ. The cells get their instructions
from this biopolymer that is Deoxyribonucleic Acid.

This information is the DNA code. This code forms due to the
sequencing of the nucleotides in the polymer chain. The DNA has very
long chains of nucleotides in their molecules and hence there are
billions upon billions of sequences possible. This is the reason all of our
DNA sequences are unique only to us.

Did you know that 99.9% of DNA is the same in all us humans? Only
0.01% of our DNA coding is special and different for every human.
This is what makes every individual unique.
Ribonucleic Acid

RNA is our second type of nucleic acid. Although it does not get as
much importance as DNA, Ribonucleic Acid is absolutely essential for
our survival. RNA is actually the blueprint of our DNAs. While the
DNA is always inside the nucleus of our cells, the RNA travels outside
the nucleus to perform its functions. There are actually three types
of Ribonucleic Acids, namely:

• Ribosomal RNA: Is the main part of the ribosome, which is where the
protein maker of our bodies.
• Messenger RNA: This RNA carries the message outside from the
nucleus. It carries the information about what type of protein cells are
to be manufactured.
• Transfer RNA: It brings the amino acid to the ribosome for protein
production.

Nucleic Acid Structure

As we have already studied Nucleic Acids are one of the most important
biomolecules present in humans. They store all our genetic information
that we pass down to future generations. And they are able to perform
their functions, due to the shape and structure they form. Let us study
about this peculiar structure of Nucleic Acids,
Just like in all biomolecules, nucleic acids are also made up of repeating
monomers. Here these repeating units or monomers have a special
name, nucleotides. These are the building blocks of nucleic acids.

Nucleotides

While discussing nucleic acid structure we must look at nucleotides.

Nucleotides are monomers that make up nucleic acids. A nucleotide
consists of three basic components. These three components are:

1] Sugar

This is typically a 5 carbon sugar. i.e a pentose. These sugars form a

bond with the phosphate groups also present in nucleotides. The sugar
in the DNA molecule is deoxyribose and the one in RNA is ribose
sugar.

2] Phosphate Group

This is the phosphates based on the inorganic compound phosphoric

acid i.e. H3PO4. They react with the sugars in the nucleotides to form
an ester bond. Nucleic acids may contain one or more of these
phosphate groups.

3] Nitrogenous Base

There are in total five nitrogenous bases. However, in the molecule of a

nucleic acid, only four are ever present.

• Adenine
• Cytosine
• Guanine
• Thymine (only present in DNA)
• Uracil (only present in RNA)
Structure of DNA

DNA is one of the two types of nucleic acids present in our bodies. You
all are well versed in DNA and the function it performs. In fact, you
have probably even seen a diagram or picture of a DNA molecule. It has
a very distinct spiral shape.

The five carbon sugar present in DNA is deoxyribose. And DNA

consists of four of the nitrogenous bases, namely Adenine, Cytosine,
Guanine and Thymine. They are expressed by the first letters of their
name A C G T. Now the nucleotides in DNA forms a link by a
dehydration synthesis polymerization method. The link forms between
the sugar atom of one nucleotide and the phosphate of the next one.
This is how the sugar-phosphate backbone of the molecule forms.

The nitrogenous bases project to the opposite side of the backbone.

DNA is composed of two such strands arranged next to each other. The
strands are anti-parallel (i.e. in opposite orientation). The nitrogenous
base of the two strands links together by hydrogen bonds. Guanine links
with Cytosine and Adenine links with Thymine. This linking plays an
important role in the replication of the DNA molecule. And this is how
DNA gets its double helix (spring-like) structure.

Structure of RNA

The lesser known of the two nucleic acids in our body is Ribonucleic
acid. It is also essential in coding and decoding of genes. Instead of
deoxyribose RNA contains the five-carbon sugar, Ribose. Also instead
of Thymine, it contains the fifth nitrogenous base of Uracil.

Similar to the DNA in RNA to the link is between the sugar and the
phosphate group. But they are single-stranded molecules and do not
typically form a helix. Unlike DNA which is permanently placed in the
nucleus, RNA molecules are more temporary. The molecules are less
stable than those of DNA.
LIPIDS

Lipids are organic compounds that contain hydrogen, carbon, and oxygen
atoms, which forms the framework for the structure and function of living
cells.”

What are Lipids?

These organic compounds are nonpolar molecules, which are soluble only in nonpolar solvents and
insoluble in water because water is polar molecules. In the human body, these molecules can
be synthesized in the liver and are and generally found in the oil, butter, whole milk, cheese, fried
foods, and also in some red meats.
Let us have a detailed look at the lipid structure, properties, types and classification of lipids.

Properties of Lipids
Lipids are a family of organic compounds, composed of fats and oils. These molecules yield high
energy and are responsible for different functions within the human body. Listed below are some
important characteristics of Lipids.

1. Lipids are oily or greasy nonpolar molecules, stored in the adipose tissue of the body.
2. Lipids are a heterogeneous group of compounds, mainly composed of hydrocarbon chains.
3. Lipids are energy-rich organic molecules, which provide energy for different life processes.
4. Lipids are a class of compounds distinguished by their insolubility in water and solubility in
nonpolar solvents.
5. Lipids are important in biological systems because they form the cell membrane, a
mechanical barrier that divides a cell from the external environment.
LIpid Structure
Lipids are the polymers of fatty acids that contain a long, non-polar hydrocarbon chain with a small
polar region containing oxygen. The lipid structure is explained in the diagram below:

Lipid Structure – Saturated and Unsaturated Fatty Acids

Classification of Lipids
Lipids can be classified into two major classes:

• Nonsaponifiable lipids, and

• Saponifiable lipids.

Nonsaponifiable Lipids
A nonsaponifiable lipid cannot be broken up into smaller molecules by hydrolysis, which includes
triglycerides, waxes, phospholipids, and sphingolipids.

Saponifiable Lipids
A saponifiable lipid contains one or more ester groups allowing it to undergo hydrolysis in the
presence of an acid, base, or enzymes. Nonsaponifiable lipids include steroids, prostaglandins, and
terpenes.
Each of these categories can be further broken down into non-polar and polar lipids.
Nonpolar lipids, such as triglycerides, are used for energy storage and fuel.
Polar lipids, which can form a barrier with an external water environment, are used in membranes.
Polar lipids include glycerophospholipids and sphingolipids.
Fatty acids are important components of all of these lipids.

Types of Lipids
Within these two major classes of lipids, there are several specific types of lipids important to
live, including fatty acids, triglycerides, glycerophospholipids, sphingolipids, and steroids. These are
broadly classified as simple lipids and complex lipids.
Also read: Biomolecules in Living Organisms

Simple Lipids
Esters of fatty acids with various alcohols.

1. Fats: Esters of fatty acids with glycerol. Oils are fats in the liquid state.

2. Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols

Complex Lipids
Esters of fatty acids containing groups in addition to alcohol and a fatty acid.

1. Phospholipids: Lipids containing, in addition to fatty acids and alcohol, a phosphoric acid
residue. They frequently have nitrogen-containing bases and other substituents, eg, in
glycerophospholipids the alcohol is glycerol and in sphingophospholipids the alcohol is
sphingosine.

2. Glycolipids (glycosphingolipids): Lipids containing a fatty acid, sphingosine, and

carbohydrate.

3. Other complex lipids: Lipids such as sulfolipids and amino lipids. Lipoproteins may also be
placed in this category
Functions OF CARBOHYDRATES

Carbohydrates are widely distributed molecules in plant and animal

tissues. In plants and arthropods, carbohydrates from the skeletal
structures, they also serve as food reserves in plants and animals. They are
important energy source required for various metabolic activities, the energy
is derived by oxidation.
Some of their major functions include:
• Living organisms use carbohydrates as accessible energy to fuel
cellular reactions. They are the most abundant dietary source of
energy (4cal/gram) for all living beings.
• Carbohydrates along with being the chief energy source, in many
animals, are instant sources of energy. Glucose is broken down
by glycolysis/ Kreb’s cycle to yield ATP.
• Serve as energy stores, fuels, and metabolic intermediates. It is stored
as glycogen in animals and starch in plants.

• They form structural and protective components, like in the cell wall of
plants and microorganisms.
• Carbohydrates are intermediates in the biosynthesis of fats and
proteins.
• Carbohydrates aid in the regulation of nerve tissue and is the energy
source for the brain.

• Formation of the structural framework of RNA and DNA (ribonucleic

acid and deoxyribonucleic acid).
• They are linked to many proteins and lipids. Such linked carbohydrates
are important in cell-cell communication and in interactions between
cells and other elements in the cellular environment.
• In animals, they are an important constituent of connective tissues.
• Carbohydrates that are rich in fiber content help to prevent
constipation.
• Also, they help in the modulation of the immune system.
The Functions of Lipids in the Body

Storing Energy
The excess energy from the food we eat is digested and incorporated into adipose tissue, or fatty
tissue. Most of the energy required by the human body is provided by carbohydrates and lipids.
As discussed in the Carbohydrates chapter, glucose is stored in the body as glycogen. While
glycogen provides a ready source of energy, lipids primarily function as an energy reserve.
Alternatively, fats are packed together tightly without water and store far greater amounts of
energy in a reduced space. Energy is needed to power the muscles for all the physical work and
play an average person or child engages in.

Regulating and Signaling

Triglycerides control the body’s internal climate, maintaining constant temperature. Those who
don’t have enough fat in their bodies tend to feel cold sooner, are often fatigued. Triglycerides
also help the body produce and regulate hormones. For example, adipose tissue secretes the
hormone leptin, which regulates appetite. In the reproductive system, fatty acids are required for
proper reproductive health. Women who lack proper amounts may stop menstruating and
become infertile. Omega-3 and omega-6 essential fatty acids help regulate cholesterol and blood
clotting and control inflammation in the joints, tissues, and bloodstream. Fats also play important
functional roles in sustaining nerve impulse transmission, memory storage, and tissue structure.
More specifically in the brain, lipids are focal to brain activity in structure and in function. They
help in forming nerve cell membranes, insulate neurons, and facilitate the signaling of electrical
impulses throughout the brain.

Insulating and Protecting

Did you know that up to 30 percent of body weight is comprised of fat tissue? Some of this is
made up of visceral fat or adipose tissue surrounding delicate organs. Vital organs such as the
heart, kidneys, and liver are protected by visceral fat. The composition of the brain is
outstandingly 60 percent fat, demonstrating the major structural role that fat serves within the
body. You may be most familiar with subcutaneous fat, or fat underneath the skin. This blanket
layer of tissue insulates the body from extreme temperatures and helps keep the internal climate
under control. It pads our hands and buttocks and prevents friction.
Aiding Digestion and Increasing Bioavailability
The dietary fats in the foods we eat break down in our digestive systems and begin the transport
of precious micronutrients. By carrying fat-soluble nutrients through the digestive process,
intestinal absorption is improved. This improved absorption is also known as
increased bioavailability. Fat-soluble nutrients are especially important for good health and
exhibit a variety of functions. Vitamins A, D, E, and K—the fat-soluble vitamins—are mainly
found in foods containing fat. Some fat-soluble vitamins (such as vitamin A) are also found in
naturally fat-free foods such as green leafy vegetables, carrots, and broccoli. These vitamins are
best absorbed when combined with foods containing fat. Fats also increase the bioavailability of
compounds known as phytochemicals, which are plant constituents such as lycopene (found in
tomatoes) and beta-carotene (found in carrots). Phytochemicals are believed to promote health
and well-being. As a result, eating tomatoes with olive oil or salad dressing will facilitate
lycopene absorption. Other essential nutrients, such as essential fatty acids, are constituents of
the fats themselves and serve as building blocks of a cell.

Note that removing the lipid elements from food also takes away the food’s fat-
soluble vitamin content. When products such as grain and dairy are processed, these essential
nutrients are lost. Manufacturers replace these nutrients through a process called enrichment.
Important Functions of
Protein in Your Body
Protein is crucial to good health.

In fact, the name comes from the Greek word proteos, meaning “primary” or
“first place.”

Proteins are made up of amino acids that join together to form long chains.
You can think of a protein as a string of beads in which each bead is an amino
acid.

There are 20 amino acids that help form the thousands of different proteins in
your body.

Proteins do most of their work in the cell and perform various jobs.

Here are 9 important functions of protein in your body.

1. Growth and Maintenance

Your body needs protein for growth and maintenance of tissues.
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Yet, your body’s proteins are in a constant state of turnover.

Under normal circumstances, your body breaks down the same amount of
protein that it uses to build and repair tissues. Other times, it breaks down
more protein than it can create, thus increasing your body’s needs.
This typically happens in periods of illness, during pregnancy and while
breastfeeding .

People recovering from an injury or surgery, older adults and athletes require
more protein as well

SUMMARY Protein is required for the growth and maintenance of tissues.

Your body’s protein needs are dependent upon your health and activity level.

2. Causes Biochemical Reactions

Enzymes are proteins that aid the thousands of biochemical reactions that
take place within and outside of your cells .

The structure of enzymes allows them to combine with other molecules inside
the cell called substrates, which catalyze reactions that are essential to your
metabolism .

.Bodily functions that depend on enzymes include :

• Digestion
• Energy production
• Blood clotting
• Muscle contraction

Lack or improper function of these enzymes can result in disease .

SUMMARY Enzymes are proteins that allow key chemical reactions to take
place within your body.
3. Acts as a Messenger
Some proteins are hormones, which are chemical messengers that aid
communication between your cells, tissues and organs.

They’re made and secreted by endocrine tissues or glands and then

transported in your blood to their target tissues or organs where they bind to
protein receptors on the cell surface.

Hormones can be grouped into three main categories :

Protein and peptides: These are made from chains of amino acids, ranging
from a few to several hundred. Protein and polypeptides make up most of
your body’s hormones.

Steroids: These are made from the fat cholesterol. The sex hormones
testosterone and estrogen, are steroid-based.

• Amines: These are made from the individual amino acids tryptophan or
tyrosine, which help make hormones related to sleep and metaboli.

• Some examples include :

• Insulin: Signals the uptake of glucose or sugar into the cell.

• Glucagon: Signals the breakdown of stored glucose in the liver.

• HGH (human growth hormone): Stimulates the growth of various

tissues, including bone.

• ADH (antidiuretic hormone): Signals the kidneys to reabsorb water.

.SUMMARY Amino acid chains of various lengths form protein and

peptides, which make up several of your body’s hormones and transmit
information between your cells, tissues and organs.
4. Provides Structure
Some proteins are fibrous and provide cells and tissues with stiffness and
rigidity.

These proteins include keratin, collagen and elastin, which help form the
connective framework of certain structures in your body .

Keratin is a structural protein that is found in your skin, hair and nails.

Collagen is the most abundant protein in your body and is the structural
protein of your bones, tendons, ligaments and skin .

Elastin is several hundred times more flexible than collagen. Its high elasticity
allows many tissues in your body to return to their original shape after
stretching or contracting, such as your uterus, lungs and arteries

SUMMARY A class of proteins known as fibrous proteins provide various

parts of your body with structure, strength and elasticity.

5. Maintains Proper pH
Protein plays a vital role in regulating the concentrations of acids and bases in
your blood and other bodily fluid.

The balance between acids and bases is measured using the pH scale. It
ranges from 0 to 14, with 0 being the most acidic, 7 neutral and 14 the
most alkaline.
A variety of buffering systems allows your bodily fluids to maintain normal pH
ranges.

A constant pH is necessary, as even a slight change in pH can be harmful or

potentially deadly .

One way your body regulates pH is with proteins.

SUMMARY Proteins act as a buffer system, helping your body maintain

proper pH values of the blood and other bodily fluids.

6. Balances Fluids
Proteins regulate body processes to maintain fluid balance.

Albumin and globulin are proteins in your blood that help maintain your body’s
fluid balance by attracting and retaining water

If you don’t eat enough protein, your levels of albumin and globulin eventually
decrease.

Consequently, these proteins can no longer keep blood in your blood vessels,
and the fluid is forced into the spaces between your cells.

As the fluid continues to build up in the spaces between your cells, swelling or
edema occurs, particularly in the stomach region .

This is a form of severe protein malnutrition called kwashiorkor that develops

when a person is consuming enough calories but does not consume enough
protein
Kwashiorkor is rare in developed regions of the world and occurs more often
in areas of starvation.

SUMMARY Proteins in your blood maintain the fluid balance between your
blood and the surrounding tissues.

7. Bolsters Immune Health

Proteins help form immunoglobulins, or antibodies, to fight infection .

Antibodies are proteins in your blood that help protect your body from harmful
invaders like bacteria and viruses.

When these foreign invaders enter your cells, your body produces antibodies
that tag them for elimination .

Without these antibodies, bacteria and viruses would be free to multiply and
overwhelm your body with the disease they cause.

Once your body has produced antibodies against a particular bacteria or virus,
your cells never forget how to make them.

This allows the antibodies to respond quickly the next time a particular
disease agent invades your body .

As a result, your body develops immunity against the diseases to which it is

exposed .

SUMMARY Proteins form antibodies to protect your body from foreign

invaders, such as disease-causing bacteria and viruses.
8. Transports and Stores
Nutrients
Transport proteins carry substances throughout your bloodstream — into
cells, out of cells or within cells.

The substances transported by these proteins include nutrients like vitamins

or minerals, blood sugar, cholesterol and oxygen .

For example, hemoglobin is a protein that carries oxygen from your lungs to
body tissues. Glucose transporters (GLUT) move glucose to your cells, while
lipoproteins transport cholesterol and other fats in your blood.

Protein transporters are specific, meaning they will only bind to specific
substances. In other words, a protein transporter that moves glucose will not
move cholesterol .

Proteins also have storage roles. Ferritin is a storage protein that stores iron (.

Another storage protein is casein, which is the principal protein in milk that
helps babies grow.

SUMMARY Some proteins transport nutrients throughout your entire body,

while others store them.
9. Provides Energy
Proteins can supply your body with energy.

Protein contains four calories per gram, the same amount of energy that carbs
provide. Fats supply the most energy, at nine calories per gram.

However, the last thing your body wants to use for energy is protein since this
valuable nutrient is widely used throughout your body.

Carbs and fats are much better suited for providing energy, as your body
maintains reserves for use as fuel. Moreover, they’re metabolized more
efficiently compared to protein .

In fact, protein supplies your body with very little of its energy needs under
normal circumstances.

However, in a state of fasting (18–48 hours of no food intake), your body

breaks down skeletal muscle so that the amino acids can supply you with
energy .

Your body also uses amino acids from broken-down skeletal muscle if
carbohydrate storage is low. This can occur after exhaustive exercise or if you
don’t consume enough calories in general

SUMMARY Protein can serve as a valuable energy source but only in

situations of fasting, exhaustive exercise or inadequate calorie intake.

The Bottom Line

Protein has many roles in your body.
It helps repair and build your body’s tissues, allows metabolic reactions to
take place and coordinates bodily functions.

In addition to providing your body with a structural framework, proteins also

maintain proper pH and fluid balance.

Finally, they keep your immune system strong, transport and store nutrients
and can act as an energy source, if needed.

Collectively, these functions make protein one of the most important nutrients
for your health.
Differences: Lipid molecules contain more energy per gram
than carbohydrates (about twice as much) Carbohydrates are more readily digested
than lipids and release their energy more rapidly. Monosaccharides and disaccharides
are water soluble and easier to transport to and from storage sites than lipids.

Carbohydrates and lipids are both types of macromolecules found in living

things. Carbohydrates are often referred to as sugars and are found in different forms
such as glucose and maltose. Lipids are fats, oils, waxes and steroids and are made
up of fatty acids.

What is the difference between carbohydrates lipids and proteins?

For instance, carbohydrates are broken down by amylase, sucrase, lactase, or
maltase. Proteins are broken down by the enzymes pepsin and peptidase, and by
hydrochloric acid. Lipids are broken down by lipases. Breakdown of these
macromolecules provides energy for cellular activities.

omparing the Biological Macromolecules

 Macromolecule Basic Formula, key features Monomer Examples

CHON

Proteins −NH2 + −COOH +R group Amino acids Enzymes, some hormones

C:H:O
Lipids Fatty acid and glycerol Butter, oil, cholesterol, beeswax
Greater than 2:1 H:O (carboxyl
group)

C:H:O Glucose, Fructose, Starch,

Carbohydrates Monosaccharides
Glycogen, Cellulose
1:2:1

CHONP
Nucleic Acids Nucleotides DNA, RNA
pentose, nitrogenous base,
phosphate

Dehydration Synthesis

Most macromolecules are made from single subunits, or building blocks,

called monomers. The monomers combine with each other using covalent bonds to
form larger molecules known as polymers. In doing so, monomers release water
molecules as byproducts. This type of reaction is known as dehydration synthesis,
which means “to put together while losing water.”

Figure 1. In the dehydration synthesis reaction depicted above, two molecules of glucose are linked together to
form the disaccharide maltose. In the process, a water molecule is formed.

In a dehydration synthesis reaction (Figure 1), the hydrogen of one monomer combines
with the hydroxyl group of another monomer, releasing a molecule of water. At the
same time, the monomers share electrons and form covalent bonds. As additional
monomers join, this chain of repeating monomers forms a polymer. Different types of
monomers can combine in many configurations, giving rise to a diverse group of
macromolecules. Even one kind of monomer can combine in a variety of ways to form
several different polymers: for example, glucose monomers are the constituents of
starch, glycogen, and cellulose.

Hydrolysis

Polymers are broken down into monomers in a process known as hydrolysis, which
means “to split water,” a reaction in which a water molecule is used during the
breakdown (Figure 2). During these reactions, the polymer is broken into two
components: one part gains a hydrogen atom (H+) and the other gains a hydroxyl
molecule (OH–) from a split water molecule.

Figure 2. In the hydrolysis reaction shown here, the disaccharide maltose is broken down to form two glucose
monomers with the addition of a water molecule. Note that this reaction is the reverse of the synthesis reaction
shown in Figure 1.

Dehydration and hydrolysis reactions are catalyzed, or “sped up,” by specific

enzymes; dehydration reactions involve the formation of new bonds, requiring energy,
while hydrolysis reactions break bonds and release energy. These reactions are similar
for most macromolecules, but each monomer and polymer reaction is specific for its
class. For example, in our bodies, food is hydrolyzed, or broken down, into smaller
molecules by catalytic enzymes in the digestive system. This allows for easy absorption
of nutrients by cells in the intestine. Each macromolecule is broken down by a specific
enzyme. For instance, carbohydrates are broken down by amylase, sucrase, lactase, or
maltase. Proteins are broken down by the enzymes pepsin and peptidase, and by
hydrochloric acid. Lipids are broken down by lipases. Breakdown of these
macromolecules provides energy for cellular activities.
 IN SUMMARY: COMPARING BIOLOGICAL MACROMOLECULES

Proteins, carbohydrates, nucleic acids, and lipids are the four major classes of biological
macromolecules—large molecules necessary for life that are built from smaller organic
molecules. Macromolecules are made up of single units known as monomers that are joined by
covalent bonds to form larger polymers. The polymer is more than the sum of its parts: it
acquires new characteristics, and leads to an osmotic pressure that is much lower than that
formed by its ingredients; this is an important advantage in the maintenance of cellular osmotic
conditions. A monomer joins with another monomer with the release of a water molecule,
leading to the formation of a covalent bond. These types of reactions are known as dehydration
or condensation reactions. When polymers are broken down into smaller units (monomers), a
molecule of water is used for each bond broken by these reactions; such reactions are known
as hydrolysis reactions. Dehydration and hydrolysis reactions are similar for all macromolecules,
but each monomer and polymer reaction is specific to its class. Dehydration reactions typically
require an investment of energy for new bond formation, while hydrolysis reactions typically
release energy by breaking bonds.

Check Your Understanding

Answer the question(s) below to see how well you understand the topics covered in the
previous section. This short quiz does not count toward your grade in the class, and
you can retake it an unlimited number of times.

Use this quiz to check your understanding and decide whether to (1) study the previous
section further or (2) move on to the next section.