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Biomolecules: Module - 7

1) Biomolecules are complex organic molecules that form the basis of life and are required for growth and maintenance of living organisms. The main classes are carbohydrates, proteins, lipids, nucleic acids, enzymes, and hormones. 2) Carbohydrates can be monosaccharides, disaccharides, or polysaccharides depending on whether they break down into one, two, or many simple sugar molecules. Glucose, fructose, and ribose are important monosaccharides. 3) Monosaccharides commonly exist as ring structures instead of open chains. Glucose preferentially forms 6-membered ring structures that can exist in alpha or beta cyclic isom

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100% found this document useful (1 vote)
64 views18 pages

Biomolecules: Module - 7

1) Biomolecules are complex organic molecules that form the basis of life and are required for growth and maintenance of living organisms. The main classes are carbohydrates, proteins, lipids, nucleic acids, enzymes, and hormones. 2) Carbohydrates can be monosaccharides, disaccharides, or polysaccharides depending on whether they break down into one, two, or many simple sugar molecules. Glucose, fructose, and ribose are important monosaccharides. 3) Monosaccharides commonly exist as ring structures instead of open chains. Glucose preferentially forms 6-membered ring structures that can exist in alpha or beta cyclic isom

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Biomolecules MODULE - 7

Chemistry of Organic
Compounds

Notes
31
BIOMOLECULES

You are aware that our body, plants and other animals are made up of many chemical
substances. There are certain complex organic molecules which form the basis of life.
These build up living organisms and are also required for their growth and maintenance.
Such molecules are called biomolecules. The main classes of biomolecules are
carbohydrates, proteins, lipids, nucleic acids, enzymes, hormones etc. In this lesson, you
will study about the structures and functions of some important biomolecules.

Objectives
After reading this lesson you will be able to :
 identify and define different types of biomolecules;
 describe the important structural features of biomolecules;
 classify carbohydrates, proteins and lipids on the basis of their structure & functions;
 give the composition of proteins and nucleic acids;
 explain the difference between DNA and RNA;
 differentiate between oils and fats;
 explain the action of enzymes and their characteristic features and
 list the functions of biomolecules in biological systems.

31.1 Carbohydrates
Carbohydrates form a very large group of naturally occurring organic compounds which
play a vital role in daily life. They are produced in plants by the process of photosynthesis.
The most common carbohydrates are glucose, fructose, sucrose, starch, cellulose etc.
Chemically, the carbohydrates may be defined as polyhydroxy aldehydes or ketones

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MODULE - 7 Chemistry

Chemistry of Organic or substances which give such molecules on hydrolysis. Many carbohydrates are
Compounds sweet in taste and all sweet carbohydrates are called as sugars. The chemical name of
the most commonly used sugar in our homes is sucrose.

31.1.1 Classification of Carbohydrates


Carbohydrates are classified into three groups depending upon their behaviour on hydrolysis.
Notes
(i) Monosaccharides: A polyhydroxy aldehyde or ketone which cannot be
hydrolysed further to a smaller molecule containing these functional groups, is known
as a monosaccharide. About 20 monosaccharides occur in nature and glucose is the
most common amongst them.
Monosaccharides are further classified on the basis of the number of carbon atoms and
the functional group present in them. If a monosaccharide contains an aldehyde group, it
is known as an aldose and if it contains a keto group, it is known as a ketose. The
number of carbon atoms present is also included while classfying the compound as is
evident from the examples given in Table 31.1. Name of some naturally occuring
monosaccharides are given in brackets.
Table 31.1 Classification of monosaccharides
No. of carbon atoms Type of monosaccharide
present Aldose Ketose
3 Aldotriose (Glyceraldehyde) Ketotriose
4 Aldotetrose ((Xylose) Ketotetrose
5 Aldopentose (Erythrose) Ketopentose
6 Aldohexose (Glucose) Ketohexose

7 Aldoheptose Ketoheptose

(ii) Disacccharides: Carbohydrates which give two monosaccharide molecules on


hydrolysis are called disaccharides e.g. sucrose, maltose, lactose etc.

(iii) Polysaccharides: Carbohydrates which yield a large number of monosaccharide


units on hydrolysis e.g. starch, glycogen, cellulose etc.

31.1.2 Structure of Monosaccharides


Although a large number of monosaccharides are found in nature, we will confine
our discussion here to four of them only viz. D-glucose, D-fructose,D-ribose and
2-deoxy-D-ribose.
D-Glucose (an aldohexose) is the monomer for many other carbohydrates. Alone or in
combination, glucose is probably the most abundant organic compound on the earth.
D-Fructose (a ketohexose) is a sugar that is found with glucose in honey and fruit juices.
D-Ribose (an aldopentose) is found in ribonucleic acids (RNA) while. 2-Deoxy-D-ribose
is an important constituent of the deoxyribonucleic acids(DNA). Here, the prefix 2-Deoxy
indicates that it lacks oxygen at carbon no. 2.
262
Biomolecules MODULE - 7
CH2OH O O
Chemistry of Organic
O Compounds
C= O C– H C– H
C– H

H – C – OH H–C–H
H – C – OH HO – C – H

HO–C–H H – C – OH
H – C – OH
H – C – OH Notes
H – C – OH H – C – OH
H – C – OH
H – C – OH H – C – OH
CH2OH
CH2OH CH2OH CH2OH

D-Glucose D-Fructose D-Ribose 2-Deoxy-D-ribose

These monosaccharides generally exist as cyclic compounds in nature. A ring is formed


by a reaction between the carbonyl group and one of the hydroxyl groups present in the
molecule. Glucose preferentially forms the six membered ring which can be in two different
isomeric forms called - and -forms (shown below as I & II). The two forms differ only
in the arrangement of the hydroxyl group at carbon No.1. Such isomers are called anomers.
Formation of these cyclic structures (I and II) from the open chain structure can be shown
as follows.

O
1 1
C–H H – C – OH
1 HO – C – H
2
H OH 2 O 2
H OH OH O
3 H
HO H 3 3
4 HO H HO H
H OH 4 4
H OH OH
5 H
H OH 5 5
H H
6
CH2OH 6 6
CH2OH CH2OH

(I)  – D – glucose (II)  – D –glucose


The cyclic structures I and II are more appropriately represented as Ia and IIa.

6 6
CH2OH CH2OH
O O
5 5
H H H H H OH
4 1 4 1
HO OH H OH HO OH H H
3 2 3 2

H OH H OH

(Ia) (IIa)
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MODULE - 7 Chemistry

Chemistry of Organic The - and -forms of other sugars also exist in the cyclic form. D-Ribose forms a five
Compounds membered ring structure as shown below

HO H2C O H HO H2C O OH
5 5
4 1 4 1
H H H H
Notes 3 2 3 2
H OH H H
OH OH OH OH
 – D – ribose  – D – ribose
D-before the name of above example indicates the configuration of particular stereoisomer.
Stereoisomers are assigned relative configurations as D– or L –. This system of assigning
the relative configuration refers to their relation with glyceraldehyde. Glyceroldehyde
contains one asymmetric carbon atom so exists in two enantiomeric forms as shown
below.

(+) –glycaraldehyde (–) –glyceraldehyde

All those compounds which can be correlated to (+) -glyceraldehyde are said to have
D-configuration and those can be correlated to (–) -glyceraldehyde are said to have
L–configuration. In monosaccharides it is the lowest asymmetric carbon atom (shown in
the box) by which the correlation is made. As in (+) glucose the lowest asymmetric
carbon atom has –OH group on the right side which matches with (+) glyceraldehyde
hence it is assigned D-configuration.

CHO

H OH

HO H
H OH CHO

H OH
H OH
CH2OH
CH2OH
(+) – glucose or (+) – glyceraldehyde or
D-glucose D-glyceraldehyde

31.1.3 Structure of Di-Saccharides and Polysaccharides


Disaccharides are formed by the condensation of two monosaccharide molecules. These
monosaccharides join together by the loss of a water molecule between one hydroxyl
264
Biomolecules MODULE - 7
group on each monosaccharide. Such a linkage, which joins the monosaccharide units Chemistry of Organic
together is called glycoside linkage. If two -glucose molecules are joined together, the Compounds
disaccharide maltose is formed.

CH2OH CH2OH
O O
H H H H H H –H2O Notes
+
HO OH H OH HO OH H OH

H OH H OH

2 molecules of  – glucose

CH2OH CH2OH
O O
H H H Glycoside H H H
linkage
O
HO OH H H H OH

H OH H H

Maltose

Similarly, sucrose (the common sugar) consists of one molecule of glucose and one molecule
of fructose joined together. Lactose(or milk sugar) is found in milk and contains one
molecule of glucose and one molecule of galactose.
If a large number of monosaccharide units are joined together, we get polysaccharides.
These are the most common carbohydrates found in nature. They have mainly one of the
following two functions- either as food materials or as structural materials. Starch is the
main food storage polysaccharide of plants. It is a polymer of -glucose and consists of
two types of chains- known as amylose and amylopectin.
Amylose is a water soluble fraction of starch and is a linear polymer of -D-glucose. On
the other hand amylopectin is a water insoluble fraction and consists of branched chain of
-D-glucose.
The carbohydrates are stored in animal body as glycogen which is also a polymer of
-glucose and its structure is similar to amylopectin.
Cellulose is another natural polysaccharide which is the main component of wood and
other plant materials. It consists of long chain of -D-glucose molecules.

31.1.4 Biological Importance of Carbohydrates


(i) Carbohydrates act as storage molecules. For example they are stored as starch in
plants and as glycogen in animals.
(ii) D-Ribose and 2-deoxy-D-ribose are the constituents of RNA and DNA, respectively.
265
MODULE - 7 Chemistry

Chemistry of Organic (iii) Cell walls of bacteria and plants are made up of cellulose. It may be of interest to note
Compounds that human digestive system does not have the enzymes required for the digestion of
cellulose but some animals do have such enzymes.
(iv) Some carbohydrates are also linked to many proteins and lipids. These molecules are
known as glycoproteins and glycolipids, respectively. These molecules perform very
specific functions in organisms.
Notes
Intext Questions 31.1
1. Name three constituents of your diet which provide carbohydrates.
2. How are carbohydrates produced in nature?
3. What are the hydrolysis products of starch and sucrose?
4. Write the linear and ring forms of D-glucose.

31.2 Proteins
Proteins are the most abundant macromolecules in living cells. The name protein is derived
from the Greek word ‘proteios’ meaning ‘of prime importance’. These are high molecular
mass complex amino acids. You will study about amino acids in the next section. Proteins
are most essential class of biomolecules because they play the most important role in all
biological processes. A living system contains thousands of different proteins for its various
functions. In our every day food pulses, eggs, meat and milk are rich sources of proteins
and are must for a balanced diet.

31.2.1 Classification of Proteins


Proteins are classified on the basis of their chemical composition, shape and solubility into
two major categories as discussed below.
(i) Simple proteins: Simple proteins are those which, on hydrolysis, give only amino
acids. According to their solubility, the simple proteins are further divided into two
major groups fibrous and globular proteins.
(a) Fibrous Proteins: These are water insoluble animal proteins eg. collagen (major
protein of connective tissues), elastins (protein of arteries and elastic tissues),
keratins (proteins of hair, wool, and nails) are good examples of fibrous proteins.
Molecules of fibrous proteins are generally long and thread like.
(b) Globular Proteins: These proteins are generally soluble in water, acids, bases
or alcohol. Some examples of globular proteins are albumin of eggs, globulin
(present in serum), and haemoglobin. Molecules of globular proteins are folded
into compact units which are spherical in shape.
(ii) Conjugated proteins: Conjugated proteins are complex proteins which on
hydrolysis yield not only amino acids but also other organic or inorganic components.
The non-amino acid portion of a conjugated protein is called prosthetic group.
Unlike simple proteins, conjugated proteins are classified on the basis of the chemical
nature of their prosthetic groups. These are
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Biomolecules MODULE - 7
Chemistry of Organic
a. Nucleoproteins (protein + nucleic acid)
Compounds
b. Mucoproteins and glycoproteins (protein+ carbohydrates)
c. Chromoproteins (proteins + a coloured pigment)
d. Lipoproteins (proteins + lipid)
e. Metalloproteins (metal binding proteins combined with iron, copper or zinc) Notes
f. Phosphoproteins (proteins attached with a phosphoric acid group).
Proteins can also be classified on the basis of functions they perform, as summarized in table
31.2.
Table 31.2 : Classification of proteins according to their biological functions
Class Functions Examples
1. Transport Proteins Transport of oxygen, Haemoglobin
glucose and other nutrients Lipoproteins
2. Nutrient and storage Store proteins required for Gliadin(wheat)
Proteins the growth of embryo Ovalbumin(egg)
Casein (milk)
3. Structural Protiens Give biological structures, Keratin(Hair, nails,etc.)
strength or protection collagen(cartilage)
4. Defence Proteins Defend organisms against Antibodies
invasion by other species Snake venoms
5. Enzymes Act as catalysts in Trypsin,Pepsin
biochemical reactions
6. Regulatory Proteins Regulate cellular or Insulin
physiological activity

31.2.2 Structure of Proteins


Protein molecules are polymers of different sizes and shapes with different physical and
chemical properties. The monomer units for proteins are amino acids. All the amino acids
that are found in proteins have an amino group(-NH2) on the carbon atom adjacent to
carbonyl group, hence are called -amino acids. The general formula of -amino acids is
shown below.
COOH
-carbon
H2 N — C — H

All proteins found in nature are the polymers of about twenty (20) different -amino acids
and all of these have L-configuration. Out of these ten (10) amino acids cannot be
synthesized by our body and hence must form the part of our diet. These are called
essential amino acids.
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MODULE - 7 Chemistry

Chemistry of Organic All proteins have one common structural feature that their amino acids are connected to
Compounds
O

one another by peptide linkages. By a peptide linkage we mean an amide (– C – N–)


H

Notes bond formed when the carboxyl group of one amino acid molecule reacts with the -
amino group of another. In the process, a molecule of water is given off. The product of
the reaction is called a peptide or more precisely a dipeptide because it is made by combining
two amino acids, as shown below:

H O H O

H — N — C — C — OH + H — N — C — C — OH

H R2
H R1

(Amino acid) (Amino acid)

H O H O

H — N — C — C — N — C — C — OH + H2O

H R1 H R2

(A dipeptide)

If a third amino acid is joined to a dipeptide in the same manner, the product is a tripeptide.
Thus, a tripeptide contains three amino acids linked by two peptide linkages. Similar
combinations of four, five, six amino acids give a tetrapeptide, a pentapeptide, a
hexapeptide, respectively. Peptides formed by the combination of more than ten amino
acid units are called polypeptides. Proteins are polypeptides formed by the combination
of large number of amino acid units. There is no clear line of demarcation between
polypeptides and proteins. For example insulin, although it contains only 51 amino acids, is
generally considered a small protein.
The amino acid unit with the free amino group is known as the N-terminal residue and the
one with the free carboxyl group is called the C-terminal residue. By convention, the
structure of peptide or proteins written with the N-terminal residue on the left and the C-
terminal on the right.
The actual structure of a protein can be discussed at four different levels.
(i) Primary structure: Information regarding the sequence of amino acids in a protein
chain is called its primary structure. The primary structure of a protein determines its
functions and is critical to its biological activity.
(ii) Secondary structure: The secondary structure arises due to the regular folding of

268
Biomolecules MODULE - 7
Chemistry of Organic
the polypeptide chain due to hydrogen bonding between and >N – H group.
Compounds
Two types of secondary structures have been reported. These are –  helix (Fig.
31.1) when the chain coils up and -pleated sheet (Fig. 31.2) when hydrogen bonds
are formed between the chains.

Notes

.
.. .
O
C One turn of the
C helix; 5.4 Aº per
.
. .. .
O turn (Pitch);
H .. .
O 3.6 amino acids
unit per turn
N H
(Pitch)
. C
.. .
O N
.
.. .
HO
C Carbon
H N
..
C .
.. .
O Oxygen
.
.. .
O
H
Nitrogen
H Side group
N Hydrogen

H N
..
N
..
Fig. 31.1 : The a-helix structure of protein

Parallel -Conformation Antiparallel -Conformation


Fig. 31.2 : The -pleated-sheet structure of protein

(iii) Tertiary structure: It is the three-dimensional structure of proteins. It arises due to


folding and superimposition of various -helical chains or -plated sheets. For example
Fig. 31.3 represents the tertiary structure for the protein myoglobin.

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MODULE - 7 Chemistry

Chemistry of Organic
Compounds

Notes

Fig. 31.3 : Structure of myoglobin

(iv) Quaternary structure: The quaternary structure refers to the way in which simple
protein chains associate with each other resulting in the formation of a complex
protein.
By different modes of bonding in secondary and tertiary structural levels a protein
molecule appears to have a unique three-dimensional structure.

31.2.3 Denaturation
One of the great difficulties in the study of the structure of proteins is that if the normal
environment of a living protein molecule is changed even slightly, such as by a change in
pH or in temperature, the hydrogen bonds are disturbed and broken. When attractions
between and within protein molecules are destroyed, the chains separate from each
other, globules unfold and helices uncoil. We say that the protein has been denatured.
Denaturation is seen in our daily life in many forms. The curdling of milk is caused by
bacteria in the milk which produce lactic acid. The change in pH caused by the lactic
acid causes denaturation, coagulation and precipitation of the milk proteins. Similarly, the
boiling of an egg causes precipitation of the albumin proteins in the egg white. Some
proteins (such as those in skin, fingernails, and the stomach lining) are extremely resistant
to denaturation.

31.2.4 Biological Importance of Proteins


(i) Proteins are structural components of cells.
(ii) The biochemical catalysts known as enzymes are proteins.
(iii) The proteins known as immunoglobins serve in defence against infections.
(iv) Many hormones, such as insulin and glucagon are proteins.
(v) Proteins participate in growth and repair mechanism of body tissues.
(vi) A protein called fibrinogen helps to stop bleeding.
(vii) Oxygen is transported to different tissues from blood by haemoglobin which is a
protein attached to haeme part.
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Biomolecules MODULE - 7
Chemistry of Organic
Intext Questions 31.2 Compounds
1. What do you understand by primary structure of protein ?
................................................................................................................................
2. What do you mean by a peptide bond?
Notes
................................................................................................................................
3. Write the general structural formula of an -amino acid?
................................................................................................................................
4. What are conjugated proteins ?
................................................................................................................................

31.3 Lipids
The lipids include a large number of biomolecules of different types. The term lipid
originated from a Greek word ‘Lipos’ meaning fat. In general, those constituents of the
cell which are insoluble in water and soluble in organic solvents of low polarity (such as
chloroform, ether, benzene etc.) are termed as lipids. Lipids perform a variety of biological
functions.

31.3.1 Classification of Lipids


Lipids are classified into three broad categories on the basis of their molecular structure
and the hydrolysis products.
(i) Simple Lipids: Those lipids which are esters and yield fatty acids and alcohols
upon hydrolysis are called simple lipids. They include oils, fats and waxes.
(ii) Compound Lipids: Compound lipids are esters of fatty acids and alcohol with
additional compounds like phosphoric acid, sugars, proteins etc.
(iii) Derived Lipids: Compounds which are formed from oils, fats etc. during
metabolism. They include steroids and some fat soluble vitamins.

31.3.2 Structure of lipids


The structure of all three types of lipids are breifly discussed below.
(i) Simple Lipids
The simple lipids are esters. They are subdivided into two groups, depending on the
nature of the alcohol component. Fats and oils are triglycerides, i.e. they are the
esters of glycerol with three molecules of long chain fatty acids. Variations in the
properties of fats and oils is due to the presence of different acids. These long chain
acids may vary in the number of carbon atoms (between C12 to C26) and may or
may not contain double bonds. On hydrolysis of a triglyceride molecule, one molecule
of glycerol and three molecules of higher fatty acids are obtained as shown below:
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MODULE - 7 Chemistry

Chemistry of Organic O
Compounds
CH2 — O — C — R1 CH2OH
O

CH — O — C — R2 H O / OH 

2
 CHOH + R1COOH + R2COOH
O
Notes + R3COOH

CH2 — O — C — R3
CH2OH
(Oil or fat)
Glycerol (Fatty acids)

By definition, a fat is that triglyceride which is solid or semisolid at room temperature and
an oil is the one that is liquid at room temperature. Saturated fatty acids form higher
melting triglycerides than unsaturated fatty acids. The saturated triglycerides tend to be
solid fats, while the unsaturated triglycerides tend to be oils. The double bonds in an
unsaturated triglyceride are easily hydrogenated to give a saturated product, and in this
way an oil may be converted into a fat. Hydrogenation is used in the manufacture of
vanaspati ghee from oils.
Fats and oils are found in both plants and animals. Our body can produce fats from
carbohydrates. This is one method that the body has for storing the energy from unused
carbohydrates. The vegetable oils are found primarily in the seeds of plants.
The second type of simple lipids are waxes. They are the esters of fatty acids with
long chain monohydroxy alcohols 26 to 34 carbons atoms. Waxes are wide-spread in
nature and occur usually as mixtures. They form a protective coating on the surfaces of
animals and plants. Some insects also secrete waxes. The main constitutent of bees wax
obtained from the honey comb of bees is myricyl palmitate:

CH3 – (CH2)14 – C – O – (CH2)29 – CH3

myricyl palmitate

The waxes discussed above should not be confused with household paraffin wax which is
a mixture of straight chain hydrocarbons.
(ii) Compound Lipids
Compound lipids on hydrolysis yield some other substances in addition to an alcohol
and fatty acids. The first type of such lipids are called phospholipids, because they
are the triglycerides in which two molecules of fatty acids and one molecule of
phosphoric acid are present. Glycolipids contain a sugar molecule in addition to fatty
acid attached to an alcohol.
(iii) Derived Lipids
Steroids are another class of lipids which are formed in our body during metabolism.
These are the compounds with a distinctive ring system that provides the structural
272
Biomolecules MODULE - 7
Chemistry of Organic
backbone for many of our hormones. Steroids do not contain ester groups and hence
cannot be hydrolysed. Cholesterol is one of the most widely distributed steroids in
Compounds
animal and human tissues.

H3 C CH3

H3 C Notes
CH3
H3 C

HO (Cholesterol)

Another important group of derived lipids is that of fat-soluble vitamins. This includes
vitamins A, D, E and K, whose deficiency causes different diseases.

31.3.3 Biological Importance of Lipids


(i) Fats are main food storage compounds and serve as reservoir of energy.
(ii) Presence of oils or fats is essential for the efficient absorption of fat soluble vitamins
A, D, E and K.
(iii) Subcutaneous fats serve as biological insulator against excessive heat loss.
(iv) Phospholipids are the essential component of cell membrane.
(v) Steroids control many biological activities in living organisms.
(vi) Some enzymes require lipid molecules for maximum action.

Intext Questions 31.3


1. What are lipids?
..................................................................................................................................
2. What are the products of hydrolysis of an oil?
..................................................................................................................................
3. Name two important types of compound lipids.
..................................................................................................................................
4. What is the basic difference between fats and oils?
..................................................................................................................................

31.4 Nucleic Acids


Why is a dog a dog and not a cat? Why do some people have blue or brown eyes and not
black? From a chemical standpoint, how does the body know what particular type of

273
MODULE - 7 Chemistry

Chemistry of Organic protein is to be synthesized? How is this information transmitted from one generation to
Compounds the next? The study of the chemistry of heredity is one of the most fascinating fields of
research today. It was recognized in the 19th century that the nucleus of a living cell
contains particles responsible for heredity, which were called chromosomes. In more
recent years, it has been discovered that chromosomes are composed of nucleic acids.
These are named so because they come from the nucleus of the cell and are acidic in
Notes nature. Two types of nucleic acids exist which are called DNA (deoxyribonucleic acid)
and RNA(ribonucleic acid).They differ in their chemical composition as well as in functions.

31.4.1. Structure of Nucleic Acids


Like all natural molecules, nucleic acids are linear polymeric molecules. They are chain
like polymers of thousands of nucleotide units, hence they are also called polynucleotides.
A nucleotide consists of three subunits: a nitrogen containing heterocyclic aromatic
compound (called base), a pentose sugar and a molecule of phosphoric acid. So a nucleic
acid chain is represented as shown below.

base base base

— Sugar — phosphate
( — sugar — phosphate
) n
— sugar —

In DNA molecules, the sugar moity is


2-deoxyribose, whereas in RNA
molecules it is ribose. In DNA, four
bases have been found. They are
adenine (A), guanine (G), cytosine (C)
and thymine (T). The first three of
these bases are found in RNA also but
the fourth is uracil (U).
The sequence of different nucleotides
in DNA is termed as its primary
structure. Like proteins, they also have
secondary structure. DNA is a double
stranded helix. Two nucleic acid chains
are wound about each other and held
together by hydrogen bonds between
Fig. 31.4 : Watson and Crick’s double helix pairs of bases. The hydrogen bonds are
structure of DNA specific between pairs of bases that is
guanine and cytosine form hydrogen
bonds with each other, whereas adenine forms hydrogen bonds with thymine. The two
stands are complementary to each other. The overall secondary structure resembles a
flexible ladder (Fig. 31.4). This structure for DNA was proposed by James Watson and
Francis Crick in 1953. They were honoured with a Nobel Prize in 1962 for this work.
274
Biomolecules MODULE - 7
Chemistry of Organic
Unlike DNA, RNA is a single stranded molecule, which may fold back on itself to form
Compounds
double helix structure by base pairing in a region where base sequences are complimentary.
There are three types of RNA molecules which perform different functions. These are
named as messenger RNA(m-RNA), ribosomal-RNA(r-RNA) and transfer RNA
(t-RNA)

31.4.2 Biological Functions of Nucleic Acids Notes


A DNA molecule is capable of self duplication during cell divisions. The process starts
with the unwinding of the two chains in the parent DNA. As the two strands separate,
each can serve as a master copy for the construction of a new partner. This is done by
bringing the appropriate nucleotides in place and linking them together. Because the bases
must be paired in a specific manner (adenine to thymine and guanine to cytosine), each
newly built strand is not identical but complimentary to the old one. Thus when replication
is completed, we have two DNA molecules, each identical to the original. Each of the
new molecule is a double helix that has one old strand and one new strand to be transmitted
to daughter cells (Fig. 3.15).

Fig. 31.5 : Replication of DNA

275
MODULE - 7 Chemistry

Chemistry of Organic Another important function of nucleic acids is the protein synthesis. The specific sequence
Compounds of bases in DNA represents coded information for the manufacture of specific proteins.
In the process, the information from DNA is transmitted to another nucleic acid called
messenger RNA, which leaves the nucleus and goes to the cytoplasm of the cell. Messenger
RNA acts as template for the incorporation of amino acids in the proper sequence in
protein. The amino acids are brought to the messenger RNA in the cell, by transfer RNA.
Notes Where they form peptide bonds. In short it can be said that DNA contains the coded
message for protein synthesis whereas RNA actually carries out the synthesis of protein.

Intext Questions 31.4


1. What is a nucleotide?
..................................................................................................................................
2. Why structure DNA is called a “doublehelix”?
..................................................................................................................................
3. Write two main structural differences between DNA and RNA.
..................................................................................................................................

31.5 Enzymes
In a living system, many complex reactions occur at the temperature of about 310K. An
example of this is the digestion of food, during which stepwise oxidation to CO2 and water
and energy production. These reactions are carried out under such mild conditions due to
presence of certain chemicals which are called enzymes. They act as catalysts for
biochemical reactions in living cells. Almost all the enzymes are globular proteins.
Enzymes are very selective and specific for a particular reaction. They are named after
the compound or class of compounds upon which they work or after the reaction that they
catalyze. The ending of an enzyme name is- ase. For example, maltase is an enzyme that
specifically catalyzes the hydrolysis of maltose into glucose. Similarly, an esterase is an
enzyme which induces hydrolysis of ester linkage.

31.5.1 Mechanism of Enzyme Action


Just like chemical catalysts, enzymes are needed only in small quantities. Similar to the
action of chemical catalysts, enzymes lower the energy barrier that reactants must pass
over to form the products. For example, hydrolysis of the ester that needs boiling with
aqueous NaOH in the laboratory, whereas it occurs at nearly neutral pH and at moderate
temperature when catalyzed by an enzyme.
There is a particular enzyme for each substrate and they are said to have lock and key
arrangement. It is said that first the substrate molecule binds to the active site of the
enzyme which results in the formation of an enzyme-substrate complex. In this complex,
the substrate is placed in the right orientation to facilitate a given reaction (Fig.31.6). This
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Biomolecules MODULE - 7
Chemistry of Organic
Compounds

Notes
Fig. 31.6 : Lock and Key arrangement of enzyme action
complex then breaks to give the molecule of the product and regenerates the enzyme for
the next molecule of the substrate.

31.5.2 Characteristics of Enzymes


(i) Enzymes speed up biochemical reactions up to ten million times compared to the
uncatalysed reaction.
(ii) Enzyme catalysed reactions rapidly attain equilibrium.
(iii) Enzymes function in dilute aqueous solutions, at moderate temperatures and at a
specific pH.
(iv) They are very specific and selective in their action on substrates.
(v) Enzymes are highly efficient and are needed in small amounts only.
(vi) In addition to the protein structure, most active enzymes are associated with some
non-protein component required for their activity, called coenzymes. For example
nicotinamide adenine dinucleotide (NAD) is a coenzyme which is associated with a
number of dehydrogenation enzymes.

Intext Questions 31.5


1. How do enzymes increase the rate of a reaction?
..................................................................................................................................
2. What do you understand by lock and key arrangement?
..................................................................................................................................

What You Have Learnt.


 Carbohydrates are polyhydroxy aldehydes or ketones or substances which provide
such molecules on hydrolysis.
 They are classified as mono-, di-and polysaccharides.
 Proteins are the polymers of -amino acids which are linked by peptide bonds.
 All proteins are the polymers of twenty different -amino acids. Out of these 10
amino acids cannot be synthesized by our body and hence must form the part of our
diet. These are called essential amino acids.
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MODULE - 7 Chemistry

Chemistry of Organic  Proteins are very important to us and perform many functions in a cell that are
Compounds absolutely necessary for our survival.
 Chief sources of proteins are pulses, milk, meat, eggs, etc.
 Biomolecules which are insoluble in water and soluble in organic solvents are called
lipids. They are classified as simple, compound and derived lipids.
 Nucleic acids are the compound which are responsible for the transfer of characters
Notes from parents to offsprings.
 There are two types of nucleic acids- DNA and RNA. They are polymers composed
of repeating units called nucleotides.
 DNA contains a five carbon sugar molecule called 2-deoxyribose whereas RNA
contains ribose.
 The four bases present in DNA are adenine, cytosine, guanine and thymine whereas
RNA contains uracil in place of thymine.
 DNA is a double strand molecule whereas RNA is a single strand molecule.
 DNA is present in the nucleus and have the coded message for proteins to be
synthesized in the cell.
 Proteins are actually synthesized by RNA which are of three types – messenger-
RNA (m-RNA), ribosomal-RNA (r-RNA) and transfer- RNA (t-RNA).
 Enzymes are biocatalysts which speed up the reactions in biosystems.
 Chemically all enzymes are proteins. They are very specific and selective in their
action on substrates.

Terminal Exercise
1. How is excess glucose stored in our body?
2. What is a disaccharide? Give an example.
3. What are the products formed by the hydrolysis of lactose?
4. What are essential amino acids?
5. Differentiate between globular and fibrous proteins with suitable examples.
6. What are triglycerides? Mention one of its important uses.
7. What is a nucleotide?
8. Differentiate between the nucleotides of RNA and DNA.
9. What are different types of RNA found in the cell? Mention their functions.
10. What are enzymes?

Answers to Intext Questions


31.1
1. Cereals, fruits and sugar.
2. Plants produce carbohydrates during photosynthesis.
3. Starch on hydrolysis gives glucose whereas sucrose on hydrolysis gives glucose and
fructose.
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