Shwetha H G[M.Sc. (organic chemistry),B.Ed.

BIOMOLECULES
The study of the chemistry of living species is called Biochemistry.
“The organic complex molecules which build the living system and maintain the growth and
reproduction of living system are called Biomolecules”
Ex: Carbohydrates proteins, nucleic acids, lipids and vitamins etc.
A.Carbohydrates
Carbohydrates maybe defined as optically active polyhydroxy aldehydes or Ketones or the
compounds which produce such compounds on hydrolysis.
Carbohydrates are also called Saccharides.(Greek: Sakcharon means sugar)
They have the general formula Cx(H2O)y
Classification of Carbohydrates:
On the basis of their behaviour on hydrolysis. They have been divided into three groups.
1) Monosaccharides
2) Oligosaccharides
3) Polysaccharides
1. Monosaccharides: Monosaccharides are the simplest carbohydrates, which can not be further
hydrolysed give simpler unit of poly hydroxyl aldehydes or ketones.
Eg: Glucose, Fructose, Galactose, Ribose, etc
2. Oligosaccharides: Oligosaccharides are the carbohydrates, which on hydrolysis to give 2 to
10 monosaccharide units.
Oligosaccharides are further classified as disaccharides, trisaccharides, tetrasaccharides, etc
a) Disacchades: Disaccharides are oligosaccharides which on hydrolysis to give two
monosaccharide units.
Eg: Sucrose, Maltose, Lactose

C12 H 22O11 
H
 C6 H12O6  C6 H12O6
Sucrose   Glucose   Fructose 
b) Trisaccharides: Trisaccharides are oligosaccharides which on hydrolysis to give three
monosaccharide units.
Eg: Raffinose
H
C18H32O16  2H2O   C6 H12O6  C6 H12O6  C6 H12O6
 Raffinose   Glucose   Fructose   Galactose 
3. Polysaccharides: Polysaccharides are the carbohydrates, which on hydrolysis to give large
number of monosaccharide units.
Eg: Starch, Cellulose, Glycogen, etc.
They have the general formula  C6 H10O5 n
 C6 H10O5 n  nH 2O 

H
 nC6 H12O6
Starch   Glucose 
Carbohydrates are further classified into 2 types based on their taste and solubility in water.
1) Sugars and 2) Non-sugars
1) Sugars : Sugars are crystalline solids soluble in water and sweet to taste.
Ex: Glucose, fructose, lactose, etc.
2) Non-sugars: Non-sugars are amorphous solids, insoluble in water and tasteless.
Ex: Starch, Glycogen.
Sugars are further classified into two types:
1) Reducing sugars: Sugars which reduces the Tollen’s reagent and Fehling’s solution on heating
are called reducing sugars.
Eg: Glucose, Maltose, Lactose, etc
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

2) Non-reducing sugars: Sugars which do not reduces the Tollen’s reagent and Fehling’s solution
on heating are called non-reducing sugars.
Eg: Sucrose

Monosaccharides:
Monosaccharides are further classified into aldoes and ketoses depending upon the functional
group present in them. The monosaccharides containing aldehyde functional group are called aldoses
and those containing ketone functional group are called ketoses.
On the basis of number of carbon atoms present in a molecule of monosaccharide, they are
further classified as
Carbon atom General term Aldehyde Ketone
3 Triose Aldotriose Ketoriose
4 Tetrose Aldoterose Ketotetrose
5 Pentose Aldopentose Ketopentose
6 Hexose Aldohexose Ketohexose
7 Heptose Aldoheptose Ketoheptose

Glucose: C6H12O6
Glucose occurs freely in nature as well as in the combined form. It is present in sweet fruits
and honey. Ripe grapes also contain glucose in large amounts (20%) hence it is called grape sugar.

Structural elucidation of Glucose:

The following factors decide the structure of glucose
1) From the elemental analysis and molecular mass determination shows that, the molecular
formula of glucose was found to beC6H12O6.
2) Glucose on heating with red phosphorus and hydroiodic acid to form n-hexane, suggesting
that all the six carbon atoms are linked in a straight chain.

HI/Red P

 CH3  CH 2  CH 2  CH 2  CH2  CH3
 n  Hexane 
3) Presence of carbonyl group CO  :
Glucose reacts with hydroxylamine to form an oxime.

Glucose reacts with hydrogen cyanide to give cyanohydrain

 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

The above reactions confirm the presence of a carbonyl group ( >C=0 ) in glucose.

4) Presence of terminal aldehydic group: CHO

Glucose on oxidation with bromine water to form gluconic acid. This indicates the presence
of terminal aldehydic group in glucose.

5) Presence of five OH groups:

Glucose reacts with acetic anhydride gives glucose penta acetate which confirms the presence
of five OH groups. Since it exists as a stable compound because five OH groups should be
attached to different carbon atoms.

6) Presence of primary alcoholic group CH2OH :

Glucose on oxidation with nitric acid to form glucaric acid or saccharic acid. This indicates
the presence of primary alcoholic group

7) Taking into account all the above facts, Baeyer in 1870 suggested the following open chain
structure for glucose.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

 The IUPAC name of Glucose is2, 3, 4, 5, 6 - pentahydroxyhexanal

 Glucose has four asymmetric carbon atoms, therefore 16 isomers are possible 2n  24  16
 The structural features of open chain structure of glucose is, that it has one aldehydic group,
two primary alcoholic group and three secondary alcoholic groups.

D and L notations of optically active isomers:

D and L system of naming the compound is based on the position of the substituent group on
the asymmetric carbon atom.
In an enantiomer the substituent group present on the right hand side of the asymmetric carbon
atom is assigned as “D” or (+).
In an enantiomer, the substituent group present on the left hand side of the asymmetric
carbon atom is assigned as “L” or ().
Eg:

If the compound contains more than one asymmetric carbon atoms then based on the
asymmetric carbon atom, the configuration is assigned.
Eg:

Glucose contains four asymmetric carbon atoms. 5th carbon atom is highest asymmetric carbon atom
on this OH group is present on the right side. Hence it is called D-glucose.
Demerits of open chain structure of glucose:
The following reactions of glucose cannot be explained by its open-chain structure.
1. Aldehydes give 2, 4-DNP test, Schiff’s test, and react with NaHSO4 to form thehydrogen
sulphite addition product. However, glucose does not undergo thesereactions.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

2. The penta-acetate of glucose does not react with hydroxylamine. This indicates that free −CHO
group is absent from glucose.
3. Glucose exists in two crystalline forms, α and β.

Cyclic structure of Glucose: (Fischer ring)

The above facts can be explained interms of cyclic structure of glucose.
During ring formation, OH group of C-5 interacts with carbonyl carbon to form a cyclic
hemiacetal structure. The ring structure can explain the existence of glucose in  and  form.

Anomers: A pair of optical isomers which differ in configuration only around C-1 atom are called
anomers.
Ex: -D-(+)-glucose and -D-(+)-glucose

Haworth structure (OR)Pyranose structure of glucose:

In 1926 Haworth propose 6 numbered ring structure for glucose based on six numbered oxygen
heterocyclic called pyrane. So Haworth structure are called Pyranose structures.

Fructose: C6H12O6(Fruit sugar)

Open chain Structure:
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

It contains ketonic functional group at C-2. It is ketohexose. It belongs to D-configurational series.

It rotates the plane polarized light to the left. So it is called Laevulose. It is written as D-(-)-fructose.
It is also called fruit sugar.

Cyclic structure of Fructose: (Fischer ring)

Fisher projection formula of -D()-fructose and -D()-fructose are

Haworth structure OR Furanose structure of Fructose: The furanose ring structure of the two
anomers of the fructose are

Disaccharides:
Sucrose (C12H22O11) (Cane sugar) :
Sucrose on hydrolysis gives equimolar mixture of D-(+)-glucose and D(-)-fructose
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

C12 H 22O11  H 2O 
 C6 H12O6  C6 H12O6
Sucrose Glu cos e Fructose

Cyclic structure OR Fischer ring structure:

“The linkage between C1 of D glucose and C2 of D fructose through oxygen atom is
called glycosidic linkage”.
The linkage between two monosaccharide units through oxygen atom is called glycosidic
linkage.”
“C1 of D glucose is linked to C2 of D fructose to form a sucrose molecule.”

Haworth structure of Sucrose

 Sucrose is a non-reducing sugar because it is made up of -(D)-glucose and -(D)-fructose.The

glycosidic linkage takes place between C-1 of glucose and C-2 of fructose so aldehydic or ketonic
group in sucrose are not free and hence it doesn’t reduce fehling solution or Tollen’s reagent.
 Sucrose is dextroraotatry after hydrolysis gives dextrorotaroty glucose and laevorotatory fructose.
Thus ‘hydrolysis of sucrose bring about a change in the sign of rotation, from dextro(+) to
laevo(-) and the product is named as Invert sugar and phenomenon is known as
inversion[Because the laevo rotation of fructose (-92.40) is more than dextro rotation of
glucose(+52.50)] .
Maltose: C12H22O11 (Malt sugar)
C1 of one Dglucose is linked to C4 of another Dglucose through oxygen atom to
form maltose.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Note:
1) Maltose is a reducing sugar.
2) Maltose contain 1, 4Glycosidic linkage.
3) Maltose hydrolysis to form two units of DGlucose.

Lactose: C12H22O11(Milk sugar)

Lactose is commonly known as milk sugar since it is found in milk. It is composed of
Dgalactose and Dglucose. It is also a reducing sugar.
“C1 of Dgalactose is linked to C4 of Dglucose through oxygen atom to form
lactose.”

( D  Galactose) (Lactose) ( D  Glucose)

 When lactose is heated Fehling’s solution or Tollen’s reagent the glucose ring breaks and free
aldehyde group is released at C-1 of glucose. So lactose is a reducing sugar.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Polysaccharides: Polysaccharides contain a large number of monosaccharide units joined together

by glycosidic linkages (Natural polymers). They mainly act as the food storage or structural materials.
Ex: starch, cellulose, glycogen.

Starch:
 Starch is the main storage polysaccharide in plants.
 Starch is the most important dietary source for human beings.
 High content of starch is found in cereals, roots, tubers and some vegetables.
 Starch is a polymer of glucose and consists of two components called Amylose and
Amylopectin.

Amylose is water soluble component which contains about 15-20% starch.

Chemically amylose is a long unbranched chain with 2001000 Dglucose units held by
C1C4 glycosidic linkage.

C1 of one glucose unit is linked to C4 of next glucose unit.

Amylopectin is insoluble in water and it contains about 80-85% of starch.

Amylopectin is a branched chain polymer of Dglucose units in which chain is formed by
C1C4 glycosidic linkage whereas branching occurs by C1C6 glycosidic linkage.

C1 of one glucose unit is linked to C4 of other glucose unit.

C1 of terminal glucose unit is linked to C6 of other glucose unit.

Differences between amylose and amylopectin:

Amylose Amylopectin
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

1. Water soluble component Water insoluble component

2. It is a long unbranched chain It is a branched chain polymer
polymer.
3. Contains 200-1000 -glycosidic It is a branched chain polymer of -D-glucose units in
linkages between C1-C4. which chain is formed by C1-C4 glycosidic linkage
whereas branching occurs by C1-C6 glycosidc linkage.
4. Constitutes about 15-20% of starch. Constitutes about 80-85% of starch.

i) Cellulose: Cellulose occurs in plants and it is the most abundant organic substance in plant
kingdom. It is a chief constituent of cell wall of plant.Cellulose is a straight chain polysaccharide
composed only of Dglucose units which are joined by glycosidic linkage between C1 of one
glucose unit and C4 of the next glucose unit.

C1 of one glucose unit is linked to C4 of next glucose unit.

ii) Glycogen:Glycogen is the main storage polysaccharide present in animals.
It is present in liver, muscles and brain, when the body needs glucose, enzymes break the
glycogen into glucose, Glycogen is also found in yeast and fungi.

Biological importance of carbohydrates:

 Carbohydrates provide energy to human beings and animals.
 Glucose present in honey acts as an instant source of energy.
 Cellulose is the fibrous component of cell walls of bacteria and plants.
 Cotton is pure form of cellulose. It is used in textile industry.
 Aldopentoses like D-ribose and 2-deoxy-D-ribose are present in nucleic acids as nucleotides.

*********
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

B. PROTEINS
Proteins are biopolymers they play important role in the development of the life process.
‘Proteins are polymers composed of monomers namely -aminoacids.’
The chief source of proteins are milk, cheese, pulses, fish, meat, etc.

Amino Acids:
Amino acids are the organic compounds containing both amino group and carboxylic group.
They have the general formula

Where: R  Hydrogen OR alkyl group OR aromatic group

Depending upon the relative position of amino group with respect to carboxyl group, the amino
acids can be classified as , ,  and  and so on.
Only amino acids are obtained on hydrolysis of proteins.

Natural Amino acids:

Sl. Name of the
Symbol Formula
No. Amino acids

1 Glycine Gly (G)

Aliphatic
2 Alanine Ala (A) aminoacids

3 Valine Val (V)

4 Leucine Leu (L)

5 Isoleucine Ile (I)

6 Arginine Arg (R)

7 Lysine Lys (K)

8 Glutamic acid Gly (E)

 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

9 Aspartic acid ASP (D)

10 Glutamine Gln (Q)

11 Asparagine ASn (N)

12 Threonine Thr (T)

13 Serine Ser (S)

14 Cysteine Sys (C)

15 Methionine Met (M)

16 Phenylalanine Phe (F)

17 Tyrosine (Y) Tyr(Y)

Try (W)
18 Tryptophan

19 Histidine His (H)

20 Proline Pro (P)

Classification of Amino acids:

 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Based on nature of amino acids they are classified into three types.

1) Acidic amino acids:

Amino acids contain more number of carboxyl groups than amino groups are called acidic amino
acids
Eg: Aspartic acid, Glutamic acid

2) Basic amino acids:

Amino acids contain more number of amino groups than carboxyl groups are called basic amino
acids
Eg: lysine, Arginine

3) Neutral amino acids:

Amino acids contain equal number of amino group and carboxyl groups are called neutral amino
acids
Eg: Glysine, Alanine

Based on the biological importance of amino acids they are classified into two types
1) Essential amino acids:
Amino acids which cannotbe synthesised in the human body are called essential amino acids
Eg: Lysine, valine, leucine

2) Non-essential amino acids:

Amino acids which can be synthesised in the human body are called non-essential amino acids.
Eg: Glycine, alanine, serine
Properties of amino acids:
1) Amino acids are colourless crystalline solids
2) They are soluble in water and have high melting points.
3) Except glycine, all other naturally occurring amino acids are optically active.

4) Zwitter ion OR Dipolar ion: In aqueous solution, the carboxylic acid group can donate a
proton to amino group giving a dipolar ion.
“The dipolar form of aminoacid which neither moves towards anode nor towards cathode
under the influence of electric field is called a Zwitter ion.”
The general form of Zwitter ion is

Eg: Zwitter ion form of alanine

5) Isoelectric point: In an
electric field, amino acid moves towards anode OR cathode depending upon the PH of the
solution and exist as a dipolar ion.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

“The PH of the solution at which the amino acid does not migrate either to the cathode
or to the anode under the influence of electric point is called isoelectric point.”

1. In Zwitter ionic form, aminoacids show amphoteric behaviour. They react both with acids and
bases.
2. Except glycine all other naturally occurring -aminoacids are optically active. Since the -
carbon atom is asymmetric.
3. These exists both in ‘D’ and ‘L’ forms. Most naturally occurring aminoacids have L-
configuration. In L-aminoacids –NH2 group is to the left of -carbon atom.

Structure of proteins:
Peptides OR peptide bond OR peptide linkage:
Peptides are compounds formed by the condensation of two OR more amino acids with the
elimination of water.

‘The amide linkage (-CONH-) between two amino acid residues in the peptide is called peptide bond.’

Dipeptide: The compound formed by the condensation of two amino acids having one peptide bond
is called dipeptide.
Eg:

Tripeptide: The compound formed by the condensation of three amino acids having two peptide
bonds is called tripeptide.

Polypeptides:If a large number of amino acids (hundreds to thousands) are joined by peptide
bonds the resulting polyamide is called polypeptide.
Eg: Insulin, Oxytocin.

Proteins:A polypeptide containing more than hundred aminoacid residues and having molecular
mass more than 10,000u is called protein. Proteins are polymers of -aminoacids. -aminoacids are
building blocks of proteins.
Ex: Albumins, Globulins, Haemoglobin, Enzymes, etc.

Classification of proteins:
On the basis of molecular structure, proteins can be classified into two types. They are
a) Fibrous proteins b) Globular proteins
a) Fibrous proteins: they consists of long polypeptide chains arranged parallel to each other and
held together by disulphide (-S-S-) and hydrogen bonds.
*Such proteins are insoluble in water. They are supporting stability to soft tissues in the animal
body.Eg: Keratin (present in hair,skin, nail), Myosin (present in muscles)
b) Globular proteins: In such proteins polypeptide chains are coiled around, giving a spherical
shape.
So globular proteins are water soluble.
Eg: Egg albumin, insulin, etc.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Structures and shapes of proteins are studied at four different levels:

Primary, secondary, tertiary and quaternary.

Primary structure of proteins: Contains one or more polypeptide chains, and each chain has amino
acids linked with each other in a specific sequence. This sequence of amino acids represents the
primary structure of proteins.

Secondary structure of proteins: Shape in which a long polypeptide chain can exist; two types of
secondary structures: α-helix, β-pleated sheet, stabilised by hydrogen bonds

α-Tertiary structure of proteins: Overall folding of the polypeptide chains; results in fibrous and
globular proteins; secondary and tertiary structures of proteins are stabilised by hydrogen bonds,
disulphide linkages, van der Waals forces and electrostatic forces.

Quaternary structure of proteins: Spatial arrangement of subunits, each containing two or more
polypeptide chains

Note:
1) Insulin contains 51 amino acids arranged in two chains A and B
2) Chain A contains 21 amino acids and are acidic in nature
3) Chain B contains 30 amino acids and are basic in nature.

Denaturation of proteins:
“The loss of physical and biological properties of a protein get changed by the action of heat,
acid, alkali or any other denaturating agent is called Denaturation of Protein”.
Denaturation changes the secondary and tertiary structure of proteins. The primary structure
remains intact.
Ex: 1) Coagulation of egg white on boiling, curdling of milk.
2) Coagulation of milk by lemon juice.

Harmones: “Hormones are molecules secreted by a endocrine glands that act as intercellular
messenger.” They produced directly in the blood stream where they control various physiological
activity such as growth or metabolism.

Classification of Harmones:
Harmones are broadly classified into three types.
1) Peptide hormones
2) Amine harmones
3) Steroid hormones.

1) Peptide hormones: Peptide hormones are made up of -aminoacid units.

Ex: a) Insulin:It is a polypeptide hormone secreted by pancreas. Its function is to lower blood glucose
level by increasing the rate of conversion of glucose into glycogen. It’s deficiency causes diabetes.
b) Oxytocin: It is a peptide hormone secreted by pituitary gland. It causes the contraction of the uterus
during child birth.
c) Glucagon: It is a peptide hormone tend to increase the glucose level in the blood.
There two hormones together regulates the normal glucose level in the blood.

2) Amine hormones: These are structurally derived from amino acids.

 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Ex: a) Adrenaline (Epineprine): It is a amine hormone produced from adrenal medulla which
stimulates the breakdown of liver glycogen into blood glucose, fats into fatty acids during emergency.

b) Thyroxine: It is an iodinated derivative of tyrosine (amino acid) produced from thyroid gland
which maintains growth and development.
Low level of thyroxine causes hypothyroidism which is characterised by lenthergyness
and obesity. High level thyoxine causes hyper thyrodism. Low level iodine in the diet leads to
hypothyroidism causes enlargement of thyroid gland. This can be controlled by using iodised salt.

3) Steroid hormones: These are produced by adrenal cortex and goands (tests in males and ovaries
in female). There are two types of steroid hormones.
i) Adrenal cortex hormones (corticoids) and
ii) Sex hormones.
i) Adrenal cortex hormones (corticoids): These are produced by the cortex of the adrenal glands.
Ex: a) Glucocorticoids: They control the carbohydrate metabolism, modulate inflammatory reaction
and involved in reactions to stress.
b) Mineralocarticoids: They control the level of excretion of water and salt by the kidney.

ii) Sex hormones: The hormones released by gonalds (tests in males and ovaries in female) which
are responsible for secondary sex characters are called sex hormones.
Ex:
a) Testosterone is the major sex hormone produced in males. It is responsible for development of
secondary male characteristics like deep voice, facial hair, general physical constitution, etc.
b) Estradiol is the main female sex hormone. It is responsible for development of secondary female
characteristics and participates in the control of menustrual cycle.
c) Progesterone is responsible for preparing the uterus for inplantation of fertilised egg.

Enzymes:Enzymes are proteins produced by living organisms to catalyse specific biochemical

reactions.
Enzymes are very specific for a particular reaction and for a particular substrate.
Ex: The enzyme which catalyses the hydrolysis of maltose into glucose is named as maltase

Vitamins:
“Vitamins are the organic compounds required in the diet in small amounts to perform specific
biologycal functions for normal maintenance of optimum growth and health of the organism.”
Vitamins are designated by alphabets A, B, C, D etc. Some of them are further named as sub
groups eg: B1, B2, B6, B12 etc. Excess of vitamins is also harmful and vitamin pills should not be taken
without the advice of doctor.

Classification of Vitamins: Vitamins are classified into two groups depending upon their solubility
in water OR oil.
1) Water soluble vitamins:
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

The vitamins which are soluble in water are called water soluble vitamins.
Eg: Vitamins B complexes –B1, B2, B6, B12, Vitamin C, etc
2) Fat soluble vitamins:
The vitamins which are soluble in fats are called fat soluble vitamins.
Eg: Vitamins A, D, E and K

Some important vitamins and their sources:

Sl. Name of
Sources Deficiency diseases
No. Vitamins
Carrots, Fish, Liver oil, Night blindness xerophthalmia
1 Vitamin-A
butter and milk (hardening of carnea of eye)
Vitamin-B1 Yeast, milk gree, vegetables Beri beri (loss of appetite, retarded
2
(Thiamine) and cereals growth)
Cheilosis (fissuring at corners of mouth
Vitamin-B2 Milk, egg white, liver,
3 and lips), digestive disorders and
(Riboflavin) kidney
burning sensation of the skin
Vitamin-B6 Yeast, milk egg yolk, cereals
4 Convulsions
(Pyridoxine) and grams
Pernicious anaemia (RBC deficient in
5 Vitamin B12 Meat, fish, egg and Curd
haemoglobin)
Vitamin-C
Citrus fruits amla and green
6 (Ascorbic Scurvy ( bleeding gums)
leafy vegetables
acid)
Rickets (bone deformities in children)
Exposure to sunlight, fish
7 Vitamin-D and osteomalacia (soft bones and joint
and egg yolk
pain in adults)
Vegetable oils like wheat Increased fragility of RBCs and
8 Vitamin-E
germ oil, sunflower oil muscular weakness
9 Vitamin-K Green leafy vegetables Increased blood clotting time

******
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

C. NUCLEIC ACIDS
Nucleic acids are the biopolymers which play an important role in storage and transmission of
genetic information and in protein biosynthesis.
There are tow types of nucleic acids
a) Deoxyribonucleic acid (DNA)
b) Ribonucleic acid (RNA)

Since nucleic acids are long chain polymers of nucleotides, so they are also called
polynucleotides.

Chemical composition of Nucleic acids:

Complete hydrolysis of DNA or RNA yields a pentose sugar, phosphoric acid and nitrogen
containing heterocyclic compounds (called bases).

D2 Deoxyribose Dribose

(a sugar present in DNA) (a sugar present in RNA)
DNA contains four bases such as adenine (A), guanine (G), Cytosine (C) and thymine (T).
RNA also contains four bases, the first three based are same as in DNA but the fourth one is uracil
(U).

Structure of Nucleic acids:

A unit formed by the attachment of a base to 11 position of sugar is known as nucleoside.

A unit formed when nucleoside is linked to phosphoric acid at 51 – position of sugar is known
as nucleotide.
 Shwetha H G[M.Sc. (organic chemistry),B.Ed.]

Note:
1. Nucleosides: The molecules in which one of the nitrogen bases is bonded with a sugar
molecule is called nucleoside.i.e, Base + Sugar = Nucleoside
2. Nucleotides: The compound formed, when the phosphate group is attached to the nucleoside
is called nucleotide.
i.e, Base + Sugar + phosphate = Nucleotide
3. A simplified version of nucleic acid chain is as shown below.

4. RNA molecules are of three types, they are named as

a) Messenger RNA (mRNA), b) Ribosomal RNA (rRNA), c) Transfer RNA (tRNA)
5. DNA double helix hold by hydrogen bonds.

Biological functions of Nucleic acids:

1. DNA molecule could make a copy of itself. This is self replication. It is very much desired for
cell multiplication and hence the growth of organisms.
2. DNA carries genetic information from generation to generation. It is a hereditary material.
3. DNA along with the three types of RNA helps in biosynthesis of proteins.
4. DNA sends genetic message required for the synthesis of specific protein through m-RNA.

Note:
Functions of RNA:
1) m-RNA carries specific information for protein synthesis from DNA by transcription.
2) t-RNA brings specific amino acids to the place of protein synthesis.
3) r-RNA is the site of protein synthesis.
********