BIOMOLECULES

Living systems are made up of various complex compounds like

Carbohydrates, Proteins, Nucleic acids ( DNA, RNA etc ), Lipids, Enzymes etc
and called “Biomolecules”. They play an important role in biochemical
reactions that occur in living systems. In addition to these, vitamins and
minerals also play an important role in the functions of organisms.

CARBOHYDRATES :-
These are the compounds primarily produced by plants. Most of them
have general formula Cx(H2O)y and are considered as hydrates of carbon from
where the name carbohydrates was derived. Ex: The molecular formula of
glucose ( C6H12O6) fits into this formula ( C6(H2O)6). But all the compounds
which fit into this formula may not be carbohydrates. For example, Acetic
acid ( CH3COOH ) fits into this formula (C2(H2O)2), but it is not a
carbohydrate. Therefore carbohydrates are defined as
Poly hydroxy aldehydes or ketones are called “Carbohydrates”.
Carbohydrates which are sweet in taste are called Sugars. Ex: Glucose,
Sucrose, Lactose. Carbohydrates are also called as “Saccharides”.

CLASSIFICATION OF CARBOHYRATES :-
Carbohydrates or saccharides are classified on the basis of their
hydrolysis into following three groups.
1. Monosaccharides :- A carbohydrate that can not be further
hydrolysed is called “Monosaccharide”. Ex : Glucose, Fructose etc.
2. Oligosaccharides :- Carbohydrates which yield two to ten
monosaccharides on hydrolysis are called “Oligosaccharides”. They are
further classified as Disaccharides, Trrisaccharides etc depending upon
number of monosaccharides they produce on hydrolysis. Amongst
theses, the most common are the disaccharides. The two
monosaccharides produced on hydrolysis of disaccharide may be same
or different. For example, sucrose on hydrolysis gives one molecule of
glucose and one molecule of fructose whereas maltose gives two
molecules of glucose only.
3. Polysaccarides:- Carbohydrates which yield large number of
monosaccharides on hydrolysis are called “Polysaccharides”. Example :
Starch, Cellulose, Glycogen etc. These are not sweet in taste, hence
they are called “Non-sugars”.
Carbohydrates are also classified as reducing and non-reducing
sugars. Carbohydrates which reduce Fehling’s solution and Tollen’s
reagent are called reducing sugars
Monosaccharides are further classified on the basis of number of carbon
atoms and the functional groups present in them. If they contain aldehyde
group, they are called “Aldoses” and if they contain keto group, they are
called “Ketoses”. The name of the monosaccharides also carries the
information about the number of carbon atoms in its molecule.

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Examples :- Aldotriose, Aldotetrose, Aldopentose, ketotriose, ketopentose.

GLUCOSE :- It is a monosaccharide occurs free in nature and also in the

form of other higher carbohydrates. It is present in fruits and honey. Ripe
grapes contain glucose in large amounts.
Preparation :-
1. From sucrose ( Cane sugar ):- Sucrose on boiling with dil HCl or
H2SO4 in alcoholic solution gives glucose and fructose in equal amounts.
+
C12 H 22O11 + H2O ⎯⎯
H
→ C6H12O6 + C6H12O6
Sucrose Glucose Fructose.

2. From Starch :- On large scale glucose is obtained by hydrolysis of

starch by boiling with dil. H2SO4 at 393 K and pressure of 2 – 3 atm.
( C6 H10O5 )n
+
+ nH 2O ⎯⎯→
H
n C6 H12O6
Starch Glucose

STRUCTURE OF GLUCOSE :- It is an aldohexose and is also known as

“Dextrose”. It is the most abundant organic compound on the earth in the
form of many higher carbohydrates. Its structure was determined on the
basis of the following facts.
1. The molecular formula of glucose is C6H12O6.
2. On prolonged heating with HI, it forms n-hexane, suggesting that all
the six carbon atoms are linked in a straight chain.

3. Glucose reacts with hydroxylamine to form an oxime and adds a

molecule of hydrogen cyanide to give cyanohydrin. These reactions
confirm the presence of a carbonyl group (>C = 0) in glucose.

4. Glucose gets oxidised to six carbon carboxylic acid (gluconic acid)

on reaction with a mild oxidising agent like bromine water. This
indicates that the carbonyl group is present as an aldehydic group.

COOH
Br2 /H2O
C

5. Acetylation of glucose with acetic anhydride gives glucose pentaacetate

which confirms the presence of five –OH groups. Since glucose exists as
a stable compound, five –OH groups should be attached to different
carbon atoms.

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6. On oxidation with HNO3, both glucose and gluconic acid yield the same
acid i.e saccharic acid which has the same number of carbon atoms as
glucose molecule has. This indicates the presence of a primary alcoholic
group in glucose.
CHO COOH COOH

(CHOH)4 Oxidation (CHOH)4 Oxidation (CHOH)4

CH2OH COOH CH2OH

Glucose Saccharic acid Gluconic acid

7. The exact spatial arrangement of different –OH groups in glucose was

given by Fischer after studying many other properties. Its configuration
is correctly represented as

CHO
H C OH
C
HO C HC
H C OH
H C OH
CH2 OH

Glucose is correctly named as D(+)-glucose. ‘D’ before the name

of glucose represents the configuration whereas ‘(+)’ represents
dextrorotatory nature of the molecule. It may be remembered that ‘D’
and ‘L’ have no relation with the optical activity of the compound. The
meaning of D– and L– notations is given as follows.
The letters ‘D’ or ‘L’ before the name of any compound indicate the
relative configuration of a particular stereoisomer. This refers to their
relation with a particular isomer of glyceraldehyde. Glyceraldehyde
contains one asymmetric carbon atom and exists in two enantiomeric
forms as shown below.

CH2OH
D(+)-Glyceraldehyde L(-)-Glyceraldehyde

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 The isomer containing –OH group on the carbon attached
to –CH2OH of the lowest position on right side in Fischer formula is
assigned as D-isomer and that with –OH group on left side is
asssigned as L-isomer.
In glucose, the carbon attached to –CH2OH group is found to
contain –OH on right side, which is similar to D(+)-Glyceraldehyde.
Therefore, the open chain structure of glucose is

CHO
H C OH
C
HO C HC
H C OH
H C OH
CH2 OH
D(+) – Glucose.

CYCLIC STRUCTURE OF GLUCOSE :- The open chain structure of glucose

explained most of its properties but fails to explain the following reactions and facts.
1. Despite having an aldehyde group, glucose doesn’t give Schiff’s test and it
doesn’t form the hydrogensulphate addition product with NaHSO3.
2. The pentaacetate of glucose doesn’t react with hydroxylamine indicating the
absence of free –CHO group.
3. Glucose is found to exist in two different crystalline forms which are named as
 and  . The  - form of glucose (m.p. 419 K) is obtained by crystallization
from concentrated solution of glucose at 303 K while  - form of glucose
(m.p.423 K) is obtained by crystallization from hot and concentrated solution
of glucose at 371 K.
The above observations could not be explained with the open chain
structure for glucose. Hence it was proposed that one of the –OH group in the
glucose molecule forms a cyclic hemiacetal structure with its –CHO group. It
was found that glucose forms a six – membered ring in which –OH group at C-
5 is involved in ring formation. This explains the absence of –CHO group and
also existence of glucose in two forms as

 -D-(+)-Glucose
The  and  forms glucose differ only in the configuration of the
hydroxyl group at C – 1 called “Anomeric carbon” and such isomers are called

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“ANOMERS”. The six membered cyclic structure of glucose is called
“Pyranose structure” in analogy with pyran. The two cyclic structures of
glucose are represented as follows.

 -D-(+)-Glucopyranose  -D-(+)-Glucopyranose

FRUCTOSE :- It is a ketohexose, obtained along with glucose by the

hydrolysis of sucrose ( a disaccharide ). Its molecular formula is same as
glucose i.e C6H12O6 containing a keto group at C-2 and six carbon atoms are
in straight chain like in glucose. It belongs to D (–) series and is a
laevorotatory compound. Its open chain structure is

Fructose also exists in two cyclic forms which are obtained by the
addition of –OH at C-5 to keto group at C-2. It forms a five membered ring
and is named as furanose in analogy with furan. The cyclic structures are
represented as

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PROTEINS :-
Proteins are polymeric compounds of amino acids and are most
abundant biomolecules of living systems. The important source of proteins
are milk, cheese, pulses, peanuts, fish, meat etc. They are present in every
part of the body and are therefore form the fundamental basis of structure
and functions of life. They are also required for growth and maintenance of
body.

AMINO ACIDS :- Amino acids contain an amino group ( –NH2 ) and carboxyl
group (–COOH ). Depending upon the relative position of amino group with
respect to carboxyl group, the amino acids are classified as  ,  ,  ,  and so
on. Hydrolysis of proteins yield only  - amino acids.  - amino acids are
generally represented as

R CH COOH
C
NH2
Where R is a side chain.
Examples :
1. Glycine (R=H)
2. Alanine ( R = CH3 )
3. Valine* ( R = (CH3)2CH ) etc.

The amino acids which can be sysnthsized in the body, are called “Non-
essential amino acids” because they can not be supplied through diet. The
amino acids which cannot be synthesized in the body and must be supplied
through diet are called “Essential Amino Acids” because it is essential to
take them through diet.
Examples of essential amino acids : Valine, Leucine, Isoleucine, Lysine etc.

Amino acids are colourless crystalline solids and are water soluble
compounds. They have high melting points and behave like salts due to the
presence of both basic amino group and acidic carboxyl group in the same
molecule. In aqueous solution, the carboxyl group can lose a proton and
amino group can accept that proton giving rise to a dipolar ion known as
“Zwitter Ion”. It is neutral but contains both positive and negative charge.

PROTEINS
These are the substances present in cytoplasm as well as in cell
membrane of the cell i.e these are the constituents of the cell. In Greek
“Proteios” means primary or holding first place. Mammalian muscle contains
about 20%, Blood plasma contains 7 %, Cow milk contains 3.5 % , cereals
contain 12 %, Beans, Nuts and pulses contain 20 % of proteins. The enzymes
and hormones which are responsible for metabolic activity of the body are
proteins. Silk, Hair, Skin, Tissues etc also contains proteins.

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 Proteins are polymeric compounds of amino acids and are most
abundant biomolecules of living systems. The important source of proteins
are milk, cheese, pulses, peanuts, fish, meat etc. They are present in every
part of the body and are therefore form the fundamental basis of structure
and functions of life. They are also required for growth and maintenance of
body.

Proteins contain C, H, O and N. The nitrogen content in protein is about

16 % of the molecular weight of proteins. These are large molecules and split
into smaller molecules by hydrolysis and the molecules are called Amino
acids. More than 700 amino acids are known to occur in nature.
Amino acids are classified as , ,  etc. Proteins are made up of 20 α –
amino acids. An infinite number of proteins are formed by the union of these
20 α – amino acids.
There are 20 important -amino acids which are present in all most all
proteins.
AMINO ACIDS :- Amino acids contain an amino group ( –NH2 ) and carboxyl
group (–COOH ). Depending upon the relative position of amino group with
respect to carboxyl group, the amino acids are classified as  ,  ,  ,  and so
on. Hydrolysis of proteins yield only  - amino acids.  - amino acids are
generally represented as

R CH COOH
C
NH2
Where R is a side chain.

Amino acid Nature of alkyl ( R ) group

1. Glycine H
2. Alanine CH3.CH –
3. Valine* [CH3]2CH–
4. Leucine* [CH3]2CH.CH–
5. Isoleucine* C2H5[CH3]CH–
6. Arginine* HN=CNH2–
7. Lysine* H2N.[CH2]4 –
8. Glutamic acid HOOC.CH2.CH2 –
9. Aspartic acid HOOC.CH2–
10. Glutamine H2N.CO.CH2.CH2–
11. Asparagine H2N.CO.CH2.CH2–
12. Threonine CH3 – CHOH –
13. Serine HO - CH2 –

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14. Cystine HS – CH2 –
15. Methionine CH3 – S – CH2 – CH2 –
16. Phenyl alanine Ph – CH2 –
17. Tyrosine
18. Tryptophan
19. Histidine 20. Proline

PROPERTIES OF AMINO ACIDS :-

1. These are colourless crystalline solids.
2. These are generally soluble in water. [ Tyrosine is soluble in hot water
and Cystine is insoluble even in hot water }
3. All naturally occuring amino acids are leavo rotatory except glysine
which has no asymmetric carbon.
4. These are highly polar. An ion is formed by the migration of proton
from –COOH to the basic –NH3 group. The ion so formed consisting of
both positive and negative charges with in the molecule and is called
“ZWITTER ION”

R – CH- COOH  R – CH – COO

NH2 NH3

5. The pH at which the zwitter ion acts as neutral and does not migrate to
cathode and anode is called “ISOELECTRIC POINT”. The isoelectric
point varies from one amino acid to the another amino acid and it
depends on different groups present in the amino acids.
6. The isoelectric point for neutral amino acids is 5.5 to 6.3
The isoelectric point for acidic amino acids is < 5
The isoelectric point for basic amino acids is > 7.

Amino acids contain an amino group and a carboxylic group and amino
group is attached to the  - carbon atom [ R – CHNH2 – COOH ]. Amino
group of one molecule react with carboxyl group of another molecule to link
two amino acid molecules by forming an amide bond called peptide linkage.
Thus the polypeptides contain a number of amino acids. Proteins are naturally
occuring polypeptides that contain more than 100 amino acid units.
However, insulin contains only 51 amino acids ( 21 in one strand and 30
amino acids in another strand)

H2N-CH-CO OH + H NH-CH-COOH H2N-CH-CO-NH-CH-COOH

R R R R

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 The amino acids containing equal number of -NH2 and – COOH groups
are called Neutral amino acids, if they contain more number of –NH2 groups
than acid groups, they are called Basic amino acids and if they contain more
number of acid groups than –NH2 groups they are called Acidic amino acids.
The amino acids which are not synthesised in the body must be supplied
through diet are called “Essential Amino Acids” and those are synthesised in
the body are called “Non Essential Amino Acids”

PEPTIDE :-
A peptide can be obtained first by activating the – COOH group of one
amino acid by converting it to it’s acid chloride or anhydride and then
allowed to react with amino group of second amino acid. The bond thus
formed between them is called “Peptide bond”. A molecule of water is lost
during the formation of peptide bond.
R.CHNH2COOH R.CHNH2COCl HNH.CHR.COOH R.CHNH2.CO.NH.CHR.COOH
POLYPEPTIDES :-
A polypeptide is formed by repeating this process. Polypeptides with
molecular weight above 10,000 are called proteins and below 10,000 are
referred to only as polypeptides.
In a polypeptide structure free amino group i.e N – terminal residue is
written on the left side and the free – COOH group i.e C – terminal group is
written on the right side of the chain as
H2N – CH[CH3] – CO – NH – CH2 – CO – NH – CH[CH3] - COOH
N-terminal C-terminal
Alanine Glycine Alanine
A polypeptide is named in such away that, the N – terminal residue
name is written first by replacing it’s suffix “ ine “ by “ yl “. The above
structure has the name “Alanylglycylalanine “. Peptides are amphoteric in
nature. A dipeptide called “Aspartame” is 160 time sweeter than sucrose
hence it is used as substitute for sugar.
H2N – CH – CO – NH – CH – COOCH3 Aspartylphenylalnine
CH2COOH CH2 – Ph methyl ester

STRUCTURE OF PROTEINS :-
Proteins are biopolymers containing a large number of amino acids
joined to each other by peptide linkage and – SH = SH – bonds having three
dimensional structure. The structure of proteins is studied under four
different levels.
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1. PRIMARY STRUCTURE :-
The amino acids in a polypeptide chain are linked with each other
in a specific sequence and this sequence is the primary structure of that
polypeptide. Any change in the sequence of amino acid is enough to
disqualify the protein from discharging it’s function. If there are 100
amino acid units in a small protein, then the 20 different amino acid
units can combine at one time in (20) 100 different ways.

2. SECONDARY STRUCTURE :-
The secondary structure of protein explains the shape of
polypeptide chain. The biological activity of protein depends on the
secondary structure. It is derived from primary structure by hydrogen
bonds between the amino acid residues close to each other.
Intra molecular hydrogen bonding occurs between the amide
nitrogen of one amino acid and carboxylic group of 4 th amino acid
residue of the polypeptide chain. In addition to the hydrogen bonds also
disulphide bonds occur either in the same chain or between the chains.
A polypeptide chain tends to fold in a repeating geometrical structure
for minimizing the energy. The secondary structure is classified into two
types as
A. α–Helical structure :
1. It is formed by the hydrogen bonds between the peptide groups
with in the same polypeptide chains.
2. It has screw type symmetry.
3. The regular appearance of the hydrogen bonds between every first
and forth peptide groups determine the regularity of turns.
4. Each turn of helix has an average of 3.6 amino acids.
B β–Pleated sheet structure :
It is formed by the hydrogen bonds between two polypeptide
chains. This bonding leads to the formation of sheets.

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3. TERTIARY STRUCTURE :-
It is three dimensional arrangement of all the atoms in the
protein. It enables the protein to form specific layers, crystals, fibres.
This tertiary structure is maintained by hydrogen bond and electrostatic
forces.
4. QUARTERNARY STRUCTURE :-
Some protein molecules are complexes containing more than one
polypeptide chains. Each chain in the molecule has its own
characteristics of tertiary structure and is called Sub – unit. The sub
units are held together by hydrogen bonding, electrostatic attraction,
hydrophobic interactions. The compound structure is called Oligomer.
Ex: Haemoglobin.

DENATURATION OF PROTEINS:-
The process of breaking up of the highly organized tertiary
structure of a protein is called “Denaturation”. The process involves breaking
up of the bonds responsible for the maintenance of three dimensional
structure. Since the bonds are weak, therefore, proteins are easily denatured.
The denaturation of proteins is determined as
1. changing the pH which disrupts the bonds.
2. Adding detergents like sodium dodecyl sulphate or organic solvents
which associates with polar groups of proteins and interfere with
hydrophobic interactions.
3. Adding reagents like urea that forms stronger hydrogen bonds with
protein groups.
4. Heating or agitation which causes disruption of attractive forces.
The biological activity of proteins is lost due to denaturation.

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 NUCLEIC ACIDS

Nucleoproteins are conjugated proteins having nucleic acids as their

prosthetic groups. Nucleoprotein is present in every living cell and in viruses
and also in bacteria. It is the essential constituent of the genes. Nucleic acids
are long chain biopolymers of nucleotides with a polyphosphate ester chain.
The two main types of nucleic acids are
1. Ribonucleic acid RNA.
2. Deoxyribonucleic acid DNA.
CHEMICAL COMPOSITION OF NUCLEIC ACIDS : -
Both the DNA and RNA are considered to be polymers of a simple units
called “ NUCLEOTIDES”. Each nucleotide is made up of a base, a sugar and
phosphoric acid. If the phosphate is removed by hydrolysis, the residue
consisting of a base and a sugar called “ NUCLEOSIDE”. The nucleoside can
be further hydrolysed to separate the base from sugar. The sugar moiety is
D-ribose in RNA and D-2- deoxyribose in DNA. Ribose is a pentose.

HC=O
HC=O

 HCOH O
O HOH2C OH
HCOH HOH2C OH 
 HCOH
HCOH
H H  H H
 H H HCOH H H
HCOH

 CH2OH OH H
CH2OH OH OH

D – ribose D-2, deoxyribose.

The two pentoses exists in the ring forms as “ Furanosides”.

BASE :-
Two types of bases are present. They are pyrimidine bases and purine
bases.
Pyrimidine bases are derivatives of pyrimidine ring. They are
CYTOSINE, URACIL and THYMINE.

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H
 NH2 O O
CH3
N N N NH

N N N O N O
O H H

Pyrimidine Cytosine Uracil Thymine

Purine bases are derivatives of purine ring. They

NH2 O

N N N
N N NH

N N N N N N NH2
H H

Purine Adenine Guanine.

DNA contains the purine bases Adenine [A], Guanine [G] and
pyrimidine bases Cytosine [C] and Thymine [T] while RNA contains purine
bases Adenine [A] and Guanine and Pyrimidine bases Cytosine [C] and Uracil
[U].
DNA AGCT
RNA AGCU
The bases combine with sugar i.e ribose or deoxyribose by C – N
linkage in which nitrogen at position-1 in case of pyrimidine and position-9 in
case of purine base and 1st carbon of sugar moiety to give necleoside. These
nucleosides combine with phosphoric acid by esterification of one of the
alcoholic groups of sugar to give nucleotide.
Adenine + Sugar Adenosine + Phosphoric acid Adenylic acid
Guanine + Sugar Guanosine + Phosphoric acid Guanylic acid
Cytosine + Sugar Cytidine + Phosphoric acid Cytidylic acid
Thymine + Sugar Thymidine + Phosphoric acid Thmidylic acid
Uracil + Sugar Uridine + Phosphoric acid Uridylic acid
Nucleoside Nucleotide.

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 NH2

O
N
N
NH
N O

N N NH2

HOH2C HOH2C

H H H H
H H H H

OH OH OH H
Cytidine D-2,deoxygunosine
A nucleotide is phosphate ester of a nucleoside. It consists of a purine
or pyrimidine base, a sugar and 1 to 3 phosphate groups. The phosphate
group is attached to 5th or 3 rd - OH group of nucleoside.
NH2
O O N
O N
-O – P – O – P – O – P – O – H2C
N N
O O- O-
-

H H
H H
OH OH

Adinosine
5 - monophosphate
Adinosine
5 - diphosphate
Adinosine
5 - triphosphate

Nucleic acids are composed of long strands of nucleotide sub – units linked by
phosphodiester bonds. The linkages join the 3 rd – OH group of one
nucleotide to the 5 th – OH group of next nucleotide. Thus a polynucleotide
is formed by the union of several nucleotides. DNA and RNA are poly
nucleotides.

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 O
O OH
-
O – P – O – H2C

O
H H
H H

O H

-
O–P O

H2C O
OH

H H
H H

OH H

DNA – A DOUBLE HELIX :-

The DNA in all the species contain bases in such away that the total
amounts of purines are equal to the total amounts of pyrimidines i.e the
amount of adenine is equal to the amount of thymine and the amount of
cytosine is equal to the amount of guanine. Therefore [ A = T ] and [ C = G ]
i.e A + G = C + T. But the AT\GC ratio varies from species to species. The
ratio is 1.52 in human beings.
Based on X – ray crystallography studies on DNA, in 1953 JD Watson
and FHC Crick proposed a double helical structure for DNA. It explains the
base equivalence and other properties of DNA.
The double helix comprises two right handed helical polynucleotide
chains [ strands ] coiled around the same central axis. The two strands are
antiparallel and their [ 5 – 3 ] phosphate linkages run in apposite directions.
The bases are placed in an order [ staked ] inside the helix in a perpendicular
direction to the helical axis. The two strands are held together by hydrogen
bonds. The reason for A = T and C = G is that adenine always pairs up with
thymine and guanine pairs up with cytosine, this is because adenine forms
two hydrogen bonds with thymine but no hydrogen bond with cytosine.
Similarly guanine can form three hydrogen bonds with cytosine but form only
one hydrogen bond with thymine.

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 The DNA strands are twisted into a helix, but the base pairs are planar
and parallel to each other on the inside of the helix. Primary structure of
nucleic acid tells about the sequence of the bases in the strand and the
secondary structure gives the double helix. The double helix resembles a
ladder with base pairs as the rungs. The hydrophobic interactions between
the staked bases are responsible for the stability of the double helix.
The diameter of the double helix is 2 nm and the double helical
structure repeats at interval of 3.4 nm. When DNA is heated the two strands
separate out. This is called melting and the temperature is called melting
temperature. Again on cooling the strands will hybridize and is called
Annealing.
RNA is also having helical structure but with single strand.

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