BIOMOLECULES

Total No.of questions in Biomolecules are-

In Chapter Examples.............................................................. 08
Solved Examples ................................................................... 12

Total No. of questions .......................................................... 20

 H
1. INTRODUCTION C12H22O11 + H2O 
 C H O +C H O
6 12 6 6 12 6

Sucrose Glucose Fructose

Molecules constituting lif e are called
Biomolecules 2. By Hydrolysis of Starch

2. CARBOHYDRATES Glucose is obtained, on commercial scale, by

hydrolysis of starch by boiling it with dilute sulphuric
Carbohydrates are defined as the optically active acid at 393 K under a pressure of 2–3 bar.
polyhydroxy aldehydes or ketones or substances H 

which yield these on hydrolysis. (C6H10O5)n + nH2O    nC H O

393 K,2  3bar 6 12 6

(a) In these compounds H : O = 2 : 1 (same as water). Starch Glucose

(b) General formula is : Cn(H2O)n or Cx(H2O)y Structure of Glucose

(c) These are also called hydrates of carbon.
The reactions of glucose indicate that its molecule
Carbohydrates contains one primary (–CH2OH) and four secondary
(>CHOH) hydroxyl groups.

CHO
Monosaccharides Oligosaccharides Polysaccharides |
(CHOH) 4
|
2.1 Monosaccharides
CH2 OH
(a) In it n = 3 to 7
(b) There naming is of following type-
Evidences that support the linear structure of Glucose
n Formula Group Aldolase Ketose
n = 3 C3H6O 3 Triose Glyceralde- Dihydroxy 1. Reduction
hyde acetone. Ni
HOH2C . (CHOH)4 . CHO + H2 
n = 4 C4H8O 4 Tetrose Erythrose Erythrulose Glucose HOCH2.(CHOH)4 . CH2OH
n = 5 C5H10O 5 Pentose Ribose Ribulose
Sorbitol
n = 6 C6H12O 6 Hexose Glucose Fructose.

2. Reaction with Hydrogen Iodide

(c) In aldolase aldehyde group is present and all
HI
central molecules are asymmetrical (chiral). HOCH2 – (CHOH)4 – CHO 
(d) In ketose, ketone group is present and except H3C – CH2 – CH2 – CH2 – CH2 – CH3
2nd carbon all molecules are asymmetrical. n-Hexane

3. Oxidation
GLUCOSE (C6H12O6) -
Br / H O
Glucose is an aldohexose. It is monomer of many HOH2C . (CHOH)4 . CHO + [O] 2 2
of the larger carbohydrates such as starch, cellulose. Glucose HOCH2 .(CHOH)4 . COOH
Gluconic acid
Preparation of Glucose
4. Acetylation
1. By Hydrolysis of Cane-sugar
OHC . (CHOH)4 . CH2OH + 5Ac2O 
In laboratory glucose can be prepared by hydrolysis Glucose Acetic anhydride
of cane-sugar in the prsence of alcohol using dilute
OHC. (CHOAc)4. CH2OAc
hydrochloric acid. Glucose and fructose are formed
Pentaacetyl glucose
in equal amounts. Glucose, being less soluble in
ethyl alcohol than fructose, crystallizes out.
5. Formation of Osazone written as:

C 6 H 5 NHNH 2
( excess )
   
 H 2O

6. Reaction with Hydroxylamine

HOCH2 – (CHOH)4 – CHO + NH2OH  Fructose also exists in two cyclic forms which
HOCH2 – (CHOH)4 – CH = N – OH +H2O are obtained by the addition of –OH at C–5 to the
Glucose monoxime
( = O) group. The ring thus formed is a five
7. Formation of Cyanohydrin membered ring and is named as furanose with
analogy to the compound furan.

HCN


Objection to linear structure :

Glucose pentaacetate does not react with hydroxyl
amine thus indicating the absence of free –CHO group.
Cyclic Structure of Glucose

H OH CH2OH The cyclic structures of two anomers of fructose

5
O are represented by Haworth structures as given
H OH
H H
O H
HO H 4 1
OH H
H OH OH 3 2 OH
H
H OH
CH2OH
 -D- Glucopyranose
 -D-(+) - Glucose
(Haworth structure)

(Fischer formula)

FRUCTOSE (LAEVULOSE), C6H12O6

Fructose is a ketohexose. It is obtained along with
glucose by the hydrolysis of sucrose..

Structure of Fructose
Fructose has the molecular formula C6H12O6 and
on the basis of its reactions it was found to contain
a ketonic functional group at C—2 and six carbon
atoms in straight chain as in case of glucose.
It belongs to D-series and is a laevorotatory
compound. Therefore, fructose is correctly named
as D-(–)-fructose. Its open chain structure may be
Isomerism glycosidic bond.
Carbohydrates which differ in configuration at the
glycosidic carbon (i.e. C1 in aldoses and C2 in Some Important Disaccharides
ketoses) are called anomers.For example, -D-
(i) Maltose = Glucose + Glucose
glucose and -D-glucose are anomers since
they differ in configuration at C 1 (glycosidic
carbon).
Carbohydrates which differ in configuration at any
H CH2OH H H CH2OH OH
carbon other than glycosidic carbon are called
epimers. For example glucose and mannose are C O C O
called epimers since they differ in configuration H H
C H C1 4C
H C
at C2 (glycosidic carbon) while glucose and OH OH
galactose are called epimers since they differ in C C C C
O
configuration at C4 (other than the glycosidic HO H
H OH H OH
carbon).

2.1.1 Derivatives of monosaccharides

Following are derivatives of monosaccharrides.
(ii) Lactose = Galactose + Glucose
(a) Deoxysugar : If 1 hydrogen occupies the position
(iii) Sucrose = Glucose + Fructose
of one – OH than deoxysugar is formed.
 It is a commercial or kitchen sugar.
H–C=O H–C=O
H–C–H H–C–OH 2.3 Polysaccharides
H–C–OH H–C–OH (a) Polysaccharides yield more than 6 molecules of
monosaccharides on hydrolysis.
H–C–OH H–C–OH
(b) General formula = (C6H10O 5)n.
H–C–OH H–C–OH
(c) These are linear polymers and also highly
OH OH branched
Deoxyribose Ribose
(d) These are not called as sugar because are
(b) Amino sugar - -OH group of Aldolase is replaced not sweet in taste.
by -NH2 group than it is called as amino sugar. Excep. - Insulin is sweet.
Eg. D-glucosamine, D-galactosamine (i) Starch
 Stored food of plant
2.2 Oligosaccharides
 It is insoluble in water.
It is formed by combination of 2 to 10 mono
saccharide units.  It gives blue colour with iodine.
 Its monomer is a -D glucose.
2.2.1 Disaccharides  It is formed of two compounds viz.
(a) The disaccharides are sugars composed of two
molecule of same or different monosaccharides.
(b) Generally one molecule of water is reduced in Amylose Amylopectin
forming disaccharides reaction is called as (a) Amylose :
dehydrogenation .
 It has 250-300 monomers.
(c) General Formula = Cn(H2O)n-1
 These are combined with  1, 4-linkage
(d) Bond present in between them is called as
  It is unbranched helical structure. (v) Sugar is structural component of DNA and
RNA.
 They give blue colour with I2 .
(vi) 1gm Carbohydrate give 4.1 kacl of energy.
 It is 15% to 20% in starch.
2.5 Test of Carbohydrates
(b) Amylopectin :
(a) Carbohydrate with Tollen’s reagent (ammonical
 Branch of 24-30 glucose monomers. silver nitrate) give silver mirror test.
 Many branchess are present. (b) Carbohydrate with Fehling solution (alkaline
CuSO4) give a red ppt.
 In straight chain it is attached by  1, 4
Examples
glycosidic bond while in branched chain it based on Carbohydrates
is linked by -1,6 linkage.
Ex.1 To classified as carbohydrate a compound
 Give red colour with I2 . must contain at least -
 It is 80 - 85% in starch. (A) 2 Carbons (B) 3 Carbons
(C) 4 Carbons (D) 6 Carbons
(ii) Glycogen (animal starch) :
Ans. (B)
 Found in form of reserved food in animals
Sol. Since carbohydrates are optically active
 It is found in more amount in Liver and polyhydroxy albehydes/ketones, it must
muscles. contain at least three carbon atoms. Hydroxy
aldehyde with 2 carbon atoms, viz. CH2 OH.
 It is a multibranched polysaccharide. CHO is not carbohydrate as it optically
 Its monomer unit is  D glucose. inactive.
 In straight chain  1,4 linkage and in branched
Ex.2 Glucose can’t be classified as-
chain  1, 6 linkage is present.
(A) Hexose
 Give red colour with I2 . (B) Carbohydrates
(C) Aldose
(iii) Cellulose (D) Oligosaccharide Ans. (D)
 It is mainly found in plant cells . Sol. Glucose is a monosaccharide, while
 It is main constituent of cell wall. oligosaccharides contain 2 to 10
monosaccharide units.
CH2OH CH2OH CH2OH
H O H O H O 3. LIPIDS
O H O H H
4 OH
OH H OH H H 1 (a) Lipids words is derived from greek word lipos
H which means fat.
H OHH H OHH H OHH
(b) Lipids are heterogeneous group of substances
Structure of Cellulose which have common property of being relatively
 It does not give colour with I2 . insoluble in water and soluble in non-polar
solvents such as ether, Chloroform etc.
 It is monomers of D-glucose
(c) Form 3-5% part of protoplasm.
  - 1,4 glycosidic bond is present
(d) H2O  2 : 1 (different from water)
 It is insoluble in water .
(e) Ratio of oxygen is less.
 Water hydrolysis is done by cellulase enzyme.
(f) Specific gravity < 1
Three types
2.4 Biological Importance of Carbohydrate :
(i) It is main source of energy.
(ii) It is called fuel of the body.
(iii) Cell wall of plant cell is made up of cellulose. Simple Compound Derived
(iv) Exoskeleton of insect is formed of chitin.
3.1 Simple lipid :  These are of two types
Simple lipid Monounsaturated - 1 Double bond is present
Eg. Oleic acid.
two types
 Oleic acid is present in more amount in
nature.
Polyunsaturated - More than two double bond
Neutral fats or Wax
Eg. Linoleic acid with two double bonds
Triglycerides
Linoleinic acid with three double bonds
3.1.1 Triglycerides
Arachidonic acid with four double bonds
(a) These are esters of fatty acids with glycerol. (Groundnut)
Ester bond is present 3.1.2 Wax :
(b) Synthesis is of following type-  These are esters of other alcohols of high
molecular weight instead of glycerols.
 These are insoluble in water.
 These are monohydric alcohols.
 Some examples of waxes -
Glycerol Fatty Acid Fats Myricye palmitate (Honeybee wax)
(c) Fatty acids which occur in natural fats usually Cetyl palmitate (Dolphin and whale wax)
contain an even number of carbon atoms (4 to Cerumen (ear wax)
30) in straight chains.
3.2 Compound Lipid- Are of 4 types :
(d) Simplest fatty acid HCOOH.
(a) Phospholipids. (b) Glycolipids.
(e) More complex fatty acid are formed by successive
addition of –CH2 groups. 3.2.1 Phospholipids :
                 Fatty acids are of 2 types Phosphorous is present.
   ex. cell wall
Saturated Unsaturated
3.2.2 Glycolipids
(i) Saturated :
 Lipid + Sugar = Glycolipids
 Only single bond is present in them.
 First member is CH3 COOH.  Present in brain, Adrenal glands, kidney,
Other examples : WBC liver, thymus, Spleen, Lungs, egg yolk
 Palmitic acid - C15 H31 COOH  Glycolipids = 2 Fatty acid + 1 sphinocine
      CH3(CH2)14 COOH
+ 1 galactose.
 Stearic acid - C17 H35 COOH
3.3 Derived lipids
    CH3(CH2 )16COOH
 Palmitic and stearic acid is found in fats of  By hydrolysis of fats they are obtained
animals in less amount.
Derived lipids
 These are solid and are found in fats. Types
(ii) Unsaturated :
Steroids Sterols
 Double bond is present in these fatty acid
chain. 3.3.1 Steroids :
 These are liquids at room temperature. Found  These are different from other fats.
in Oils.
  It is insoluble in water. 'R' group attach with the carbon than that carbon
(i) Bile acids  is called  - carbon.

 Present in secretion of liver. H

(ii) Sex hormones : NH2–C–COOH or NH2–CH2–COOH
 These are androsterones. H
Glycine
(iii) Adrenal hormone- Eg : Aldosterone
3.3.2 Sterols : CH2OH CH3
 They have -OH groups. NH2–C–COOH NH2–C–COOH
 They are complex monohydroxy alcohols. H H
(i) Cholesterol - It is widely distributed in all cells Serine Alanine
of body.
(c) Amino acids have also NH2 group. Which is basic
3.4 Biological importance of Fat : and also COOH group. Which is acidic. So Nature
of Aminoacid is Acidic + Basic
 It is source of energy.
(d) Amino Acids are amphoteric in nature. So for it
 It is important for absorption of vitamin A, D,
E and K. a special term is coined called Zwitter ion.

 It is important component of plasma (e) They have following structure in solution

membrane.
R
 It act as shock absorber of body.
+
H 3N–C–COO –
 Calorific value 9.3 kcal.
H

4. PROTEINS [Zwitter Ion]

[Net charge on it is zero]
(a) Proteins are polymers of amino acids.
(b) Protein is 3/4 part of dry weight of tissues.
4.2 Classification of Amino Acids :
(c) Protein forms structure of body.
(A) According to synthesis amino acid is of two
(d) C, H, O, N are necessary present in proteins. types-
(e) In some proteins P, S, Fe, Cu, I, also may be (i) Essential amino Acids :
present. They are called trace elements.
(f) 70 types of Amino acids are known. But in  These are taken by food. Not synthesized in
proteins about 20 types of amino acids are used. the body.
other amino acids are called non-proteinious
amino acid for e.g. citruline, ornithine  These are as follows
4.1 Chemical Structure : (1) Leucine (2) Isoleucine
(a) Amino acids can be given by the general formula.
(3) Lysine (4) Methionine
R R
(5) Phyenyl alanine (6) Threonine
H2N–C–C–OH or H2N–C–COOH
(7) Tryptophan (8) Valine
H O H
R = Alkyl group. Arginine and Histidine are semiessential amino
acids ie. they are bartly synthesized in tissues.
(b) If 'R' Changes amino acids formed also changes.
e.g. If R = H  Glycine (Simplest A. Acid) (ii) Non - Essential Amino Acid :
If R = CH3  Alanine (a) These are synthesized in body.
If R = CH2OH  Serine.
(b) These are not required in food.
 (c) These are as follows 4.4 Configuration of proteins :
(1) Alanine (2) Aspargine (a) Biological nature or function of protein was
confirmed by its conformation.
(3) Aspartic acid (4) Cistine
(b) This conformation is of 4 types
(5) Glutamic acid (6) Glutamine
(7) Hydroxy proline (8) Glycine Primary Secondary Tertiary Quaternary
(9) Proline (10) Serine
4.4.1 Primary Structure :
(11) Tyrosine
 This type of structure was given by Friedrich
(d) Except glycine all Amino Acid has 2 optical Sanger in 1953 in Insulin (of one chain)
image (1 and 2)
 Primary structure is conformed by a single
(e) Optical isomerism are those which has a polypeptide chain in a linear manner.
simmilar common formula but there images  All amino acid are attached in a straight chain
opposes to each other. by peptide bond.
(f) For it chiral carbon atom is necessary. Chiral  No biological importance & soon changed to
carbon atom is that carbon atom whose four other forms.
valency are not satisfied by same group or ,

atoms.
4.4.2 Secondary Structure :
(g) In Glycine chiral carbon atom is absent. It is  In it structure of straight chain from irregular
optically inactive. changes to form coils.
(h) L-form synthesize protein.  H-bond + peptide bond present in secondary.
structure.
4.3 Peptide bond :  This H bond is present between hydrogen of
Amino group and oxygen atom carboxylic
(a) Two or more than two amino acid linked and form acid group.
a peptide.
 This structure is of two types
(b) The bond present in between peptides is called
peptide bond.
It is of 3 types -helix - pleated sheet

Dipeptide Tripeptide Polypeptide

C
(nAA = 2) (nAA = 3) (nAA > 3) N
O N N
(c) A peptide bond is bond between -NH3 of one C RCH RCH RCH
C
54 pm

Amino acid and -COOH of another amino acid. O C C C O

HO H N O O
C H H N H N
R R N HCR
| | O C HCR HCR
N
H O C
H– N – C – C – O  H  H – N – C – C –OH C O
C
H C O N H O N H H
| | || | | || C N N
O RCH
H H O H H O O
RCH RCH
N C C
H H H O O C O
Amino Acid Amino Acid N N H N H N
HCR HCR
R R H N HCR
C C C
H O
| | N
2 H – N – C – C – N – C – C –OH
| | || | | ||
H H O H H O (i)  - helix
 Chain is spiral
Peptide  3.7 atoms in one coiling
Bond
 Right handed circular.
Formation of Peptide Bond
Eg.  Myosin, Keratin etc.
 (ii)  -pleated sheet 4.5 Types of proteins
 Structure of protein is not arranged in a  Classification of protein is based upon three
sequence. general properties shape, Solubility and
 Polypeptide chain are parallel to each other Chemical composition.
 H - bond form by near chains Proteins
Eg. Silk fibres.  
4.4.3 Tertiary structure :
                                           
 In this structure of protein atoms are highly
coiled and form a spherical form Simple Conjugated Derived
Ex. Albumin
 This structure is formed by 4 regular hydrogen 4.5.1 Simple proteins
bonds which makes a regularity in it  It is formed of only Amino Acids
(i) Hydrogen bond :  Types

|  
C = O........H — N —
| | Fibrous Globular
H (A) Fibrous :
Hydrogen bond
 It is insoluble
 They are formed between oxygen of acidic
amino acid and H of basic amino acid.  It is of elongated shape.
(ii) Hydrophobic bond -  It is highly resistant to digestion by proteolytic
 Non - polar side chains of neutral amino acid enzymes.
tends to be closely associated with one  Their main function - Protection.
another in proteins. Ex. Collagen, Keratin etc
 Present in between the amino Acid. (B) Globular :
 These are not true bonds.
 These are spherical and oval in shape.
(iii) lonic bond : Chains are highly coiled
– COO–.....H3+N–  These are soluble.
Ionic bond Ex. Albumin
 These are salt bonds formed between
oppositely charged groups in side chains of 4.5.2 Conjugated Proteins
Amino acids  These are complex proteins in which protein
Eg. Aspartic acid molecule is combined with characteristic non-
amino acid substance.
Glutamic acid
 Non-amino acid or Non - Protein part is called
(iv) Disulphide bonds : as prosthetic group
| ------ S - S ---- | Ex. Nucleoproteins
 Relatively stable bond and thus is not broken (Protein + Nucleic acid),
readily under usual conditions of denaturation.
Phosphoproteins (Protein + (PO3)2– )
 Formed between the -SH group of Amino acid Eg.  Casein of milk., Vitelline of egg - yolk
Ex.Cystine and Methionine .
4.4.4 Quaternary structure : 4.5.3 Derived proteins :
 When 2 or more polypeptide chains united
by forces other than covalent bonds (i.e. not (a) These are obtained as a result of partial
peptide and disulphide bonds) are called hydrolysis of natural proteins.
Quaternary structure.
Eg.  Proteose, Metaproteins, Peptones
 It is most stable structure.
(b) Denaturation of Proteins
Ex. Haemoglobin
When a protein in its native form, is subjected to a
 physical change like change in temperature, or a 5. NUCLEIC ACID
chemical change like change in pH, the native
(a) These are special type of acids which are present
conformation of the molecule is disrupted and
in nucleus & cytoplasm.
proteins so formed are called denaturated proteins.
(b) Control the metabolic activities of cell.
The denaturation may be reversible or irreversible. (c) They are also found in Mitochondria, centriole
The coagulation of egg on boiling is an example of and chloroplast.
irreversible protein denaturation. Types  These are of 2 types
However, it has been shown now that in some cases, DNA (Deoxyribonucleic acid)
the process is actually reversible. The reverse
process is called renaturation. RNA (Ribonucleic acid)

4.6 Test of Protein : (d) Fischer discovered Nitrogen bases in 1888

(a) With conc. HNO3 on heating give yellow ppt.
Which on more heating give solution On adding Nitorgen Base
NH4OH Red colour appears. It is Xanthoprotic types
test.
Purine Pyrimidine
(b) (NH4OH) + dil. CuSO4 protein give Blue violet
colour. It is a biurete test.
(e) Levan found sugar
4.7. Biological Importance of protein :
2 types
(a) Component of plasma membrane.
(b) All enzymes are protein. Ribose (RNA) Deoxyribose (DNA)
(c) Many hormones are protien.
(d) Antigen and antibody are protein.
(e) Actin and myosin protein are important in muscle 5.1 Deoxyribosenuclic Acid (D.N.A.):
contraction. (a) It is found in Nucleus.
(f) Proteins are important in growth, regeneration and
(b) They on pneumococcus bacteria.
repairing.
(g) Calorific value 4.0 kcal. (c) DNA made up of 3 units-

               
Examples
based on Proteins Nitrogen base Deoxyribose Phosphoric acid

Ex.3 Relation between amino acids and proteins   sugar (H3PO 4 )

is smililar to the one present between-     
(A) Glucose and fructose                
(B) Thyamine and uracil Pyrimidine Purine.
(C) Glucose and Glycogen (i) Thymine (i) Adenine
(D) Glucose and lactose Ans.(C) (ii) Cytosine (ii) Guanine
(d) Nucleoside
Sol. Proteins are formed of amino acids so the
same relation as in glucose and glycogen. When nitrogen base combined with deoxyribose
sugar it constitute a nucleoside.
Ex.4 Which of the following is proteins - S.No. Deoxyribonucleoside
(A) Nylon (B) Terry cotton
1 Adenine + Deoxyribose  Deoxyadenosine
(C) Natural silk (D) Rayon Ans.(C)
2 Guanine + Deoxyribose  Deoxyguanosine
Sol. Silk has  pleated structure. 3 Cytosine + Deoxyribose  Deoxycytidine
4 Thymine + Deoxyribose  Deoxythymidine
(i) Nucleotide (ii) Protein Synthesis
(a) Nitrogen base+Sugar+Phosphate Nucleotide The specific sequence of base pair in DNA
represents coded information for the manufacture
(b) Nucleotide is a unit of DNA. of specific proteins. These code instructions first
(c) All nucleotides combined and form a chain called are transcribed into the matching nitrogen- base
polynucleotides by which RNA and DNA formed. sequences within mRNA and the instructions in
such RNA subsequently are translated into
5.1.1 Structure of DNA particular sequence of amino acid units within
(a) Double Helical model of DNA was proposed by the polypeptide chains and proteins.
biochemist J.D.Watson, British chemist The major steps in the utilization of the genetic
FHC Crick in 1953. information can be represented as :
Transcription
D N A Re

plication
 D N A   R N A
5' 2 3 Translation
P 1    Protein
5 4 S T A S 4
3 2 1 P 3'
5 P 5 5.2 Ribonucleic Acid (R N A ) :
S C G S
 Found in cytoplasm as well as in nucleus.
P 5
5 P 1
S Cytoplasm  In the ribosome (heigher
3' 4 S G C
amount)
3 2 P 5
Structure of DNA 5' 5.2.1 Chemical Nature :
 Ribonucleic acid is a polymer of purine and
pyrimidine ribonucleotides linked by 3'  5'
(b) DNA in double stranded structure is made up of
phosphodiester bridges.The number of
two chains of polynucleotides.
nucleotides in RNA ranges from as few as
(c) DNA is a polymer of Nucleotide. 75 to many thousands. Although sharing
(d) Nucleotide are joined by 3'  5' phosphodiester many features with DNA, RNA possesses
bonds. several specific difference.
 As indicated by its name, sugar in RNA to
(e) Sugar and phosphorous are alternately arranged.
which the phosphate and nitrogen- bases are
(f) In both chains, in between A and T, 2 Hydrogen attached is ribose rather than the deoxyribose
bonds are present while in C and G 3H bonds of DNA.
are present. (A = T) (C  G)  Although RNA contains the ribonucleotides
(g) A always attach with T while C always attaches of adenine, guanine, and cytosine, it does
with G. not posses thymine. Instead of thymine, RNA
contains the ribonucleotides of uracil. Thus
(h) Purine and pyrimidine are found in ratio 1 : 1.
the pyrimidine components of RNA differs
cells. from those of DNA.
(i) DNA is attached with histone protein.  RNA exists basically as a single-stranded
(j) In prokaryotic cell and mitochondria circular DNA molecule rather than as a double -stranded
is present. helical molecule, as does DNA. However the
single strand of RNA is capable of folding
back on itself like a hairpin and thus acquiring
5.1.2 Function of DNA double-stranded characteristics. In these
(i) Self - Replication or self -Duplication regions. A pairs with U and G pairs with C.
Thus a given segment of a long RNA molecule
DNA has the property of self - replication . It is
might, for example, be represented as follows.
therefore a reproducing molecule. This unique
property of DNA is at the root of all reproduction. P – R–P–R – P –R –P –R–P– R
Through its replication, DNA is acts as the key | | | | |
to heredity. In the replication of DNA, the two A U G G C
strands of a double helix unwind and separate as  where R stands for ribose ; A, U, G, and C
a template f or the f ormation of a new for Adenine, Uracil, Guanine and Cytosine
complementary strand. respectively.
5.2.2 Types of RNA and their Functions : Ex.6 Which one of the following is not present in RNA-
There are 3 main types of RNA molecules (A) Uracil (B) Thymine
(i) Messenger RNA (mRNA) (C) Ribose (D) Phosphate
(ii) Transfer RNA (tRNA)
Ans. (B)
(iii) Ribosomal RNA (rRNA)
Sol. Except thymine all Uracil, Ribose &
(i) Messenger RNA (mRNA) phosphate are present in R.N.A.

 This type of RNA consists of single strand

of variable length and serves as a template 6. ENZYMES
for protein synthesis. Codon in the
chromosomes. Proteins which are used as a catalyst in
 mRNA forms complementary copy of DNA biochemical reaction is known as biocatalysts.
as it carries chemical messages in the
form of nitorgen- base sequence from the 6.1 Specific cheracteristics
nucleus to the ribosomes, i.e. from DNA Enzymes have following two specific character
to cytoplasm where proteins are as :
synthesized. Theref ore, it is called
messenger RNA or mRNA (i) Specificity (ii) Efficiency
6.1.1 Specificity of enzymes
 mRNA is sythesised from DNA in the (a) Generaly one enzyme can catalyze only one
nucleus. It is called transcription. biochemical reaction.
(b) It can increases rate of reaction upto 1020 times.
(ii) Ribosomal RNA
(c) In some cases one enzyme can catalyzes more
 A ribosome is a cytoplasmic nuucleoprotein
structure which serves as the organellar than one reaction and one reaction can be
machinery for protein synthesis from mRNA catalyzed by more than one enzyme.
templates. eg. Enzyme present in Yeast (Zymase) can
 On the ribosome, the mRNA and tRNA ferment both glucose and fructose into alcohol
molecules interact to translate into a specific and also cane-sugar can be hydrolyses by
protein molecule the information transcribed invertase and sucrase enzymes.
from the DNA.
6.1.2 Efficiency of enzymes
 rRNA constitutes the largest part of total RNA
(Highest) - 80% (a) One molecule of enzyme can convert millions of
(iii) Transfer RNA (tRNA) : substrate molecules into product per second.
 These are also called Soluble RNA. eg. Carbonic anhydrase enzyme present in red
 Single stranded. blood cells has a highest turn over number.

 10-15% of the total RNA. (b) With having tertiary structure it can be collected
as crystals.
 Size - Smallest  75 - 80 nucleotides only.
 Synthesis - Within nucleus from DNA. Enzymes are denatured at higher temperature.

Function- It transport amino acid from cyto (c) Enzyme can be stored at low temperature as
plasm to the site of protein synthesis. they are inactivated.
Examples 6.2 Importance of enzymes
based on Nucleic acid
In the thousands of enzymes presents in body if
Ex.5 Which of the following sugar is present in even a single enzyme would be absent or
R.N.A.- damaged than complex disease in results.
(A) Ribose (B) Deoxyribose
eg. Scarcity of Phenylalanine hydroxylase
(C) Both (D) None Ans. (A) enzyme in human body is result in
Sol. Ribose C5H10O 5 Phenylketonuria disease.
6.3 Factors affecting enzyme action : 7. NUTRIENTS
(i) Optimum temperature and pH. Enzyme catalysed Sodium, Potassium and Chlorine
reactions have maximum rate at physiological pH
(i) Na+ is the principal mineral cation in the extracellular
of around 7.4 and human body temperature of 37ºC
fluid.
(310 K) under one atmosphere pressure.
In fact, as the temperatue or pH is increased, the (ii) K+ is the principal cation inside the cell.
rate rises to a maximum (at 37ºC or pH = 7.4) and (iii) Cl– is the principal mineral anion in the ECF.
then falls off.
(iv) Na+ and K+ are essential to the maintenance of water
(ii) Enzyme activators (co-enzymes). The balance and acid-base balance.
activity of certain enzymes is increased in the
presence of certain substances, called co-enzymes. (v) Na + and K + are important in nerve impulse
transmission.
It has been observed that if a protein contains a
small amount of vitamin as the non-protein part, its Calcium and Phosphorus
activity is enhanced considerably. The activators are
(i) Calcium and phosphorus are deposited in bones and
generally metal ions such as Na+, Mn2+, Cu2+, Co2+
teeth to give them strength and rigidity.
etc. These metal ions are weakly bonded to the
enzyme molecules and increase their catalytic (ii) Ca 2+ is also essential for blood coagulation,
activity. For example, the enzyme, amylase, in neuromuscular function, cardiac function and actions
presence of NaCl, which provides Na+ ion, shows a of many enzymes and hormones.
very high catalytic activity. (iii) Phosphorus enters into many compounds such
(iii) Enzyme inhibitors and poisons. Just as in the as nucleic acids and phospholipids, many
case of catalysts, the activity of enzyme is slowed coenzymes and high energy compounds like
ATP.
down in the presence of certain substance. Such
substances are called inhibitors or poisons. They (iv) Calcium plays an essential role in sustaining
act by combining with the active functional group intestinal peristalsis and growth of body tissues.
thereby reducing or completely destroying the
Iron
catalytic activity of the enzymes. The use of many
drugs is on account of thier action as enzyme (i) Iron is required for haemoglobin synthesis.
inhibitors in our body. (ii) Iron is essential both for transportation of
Examples oxygen to tissues and for operation of oxidative
based on Enzyme
systems within the tissue cells.
Ex.7 Enzyme is made up of - Magnesium
(A) Proteins (B) Minerals
(i) Magnesium is required as a catalyst for many
(C) Oil (D) Fatty acids intracellular enzymatic reactions, particularly
Ans(A) those relating to carbohydrate metabolism.

Sol. All enzymes are proteins (ii) Mg is the central metal atom in chlorophyll

Iodine
Ex .8 The enzyme which catalyses hydrolysis of
sucrose is- Iodine is used in the synthesis of thyroid hormones.
(A) Maltase (B) Zymase Zinc
(C) Invertase (D) Proteinase
(i) Zinc is a constituent of carbonic anhydrase,
Ans(C) present in RBCs helping in CO2 transport.
Sol. Hydrolysis of sucrose is called inversion. (ii) Zinc is a component to lactic dyhydrogenase,
important for the interconversion between pyruvic
 acid and lactic acid Some important vitamins, their sources and
diseases caused by their deficiency are listed in
(iii) Zinc is a component part of some peptidases
table.
and therefore is important for digestion of proteins
in the alimentary canal
Sr. Name of Source Deficiency
Cobalt No Vitamins Diseases
(i) Cobalt helps in erythropoiesis and in the .
activities of some enzymes. 1 Vitamin A Fish liver Xerophthalmia
(Retinol) oil, carrots, (hardening of
(ii) It is present in vitamin B12 . butter and cornea of eye)
Copper milk Night blindness
2 Vitamin B1 Yeast, milk, Beri beri (loss of
(i) Copper helps in the utilisation of iron. Green appetite,
(Thiamine)
(ii) Copper deficiency may produce anaemia vegetables retarded growth)
because of failure in iron utilisation. and cereals
and grams
Molybdenum
(i) Molybdenum is a constituent of oxidase
enzymes (xanthine oxidase) 3 Vitamin B2 Milk, Cheilosis
(Riboflavin) eggwhite, (fissuring at
(ii) Molybdenum plays an important role in
liver, Kidney corners of
biological nitrogen fixation
mouth and lips),
Fluorine digestive
disorders and
(i) Fluorine maintains normal dental enamel and
burning
prevents dental caries.
sensation of the
(ii) Exessive intake of fluorine cause fluorosis skin
characterized by mottled teeth and enlarged 4 Vitamin B6 Yeast, milk, Convulsions
bones. (Pyridoxine) egg yolk,
cereals
and grams
8. VITAMINS
It has been observed that certain organic compounds 5 Vitamin B12 Meat, fish, Pernicious
are required in small amounts in our diet but their (Cyanocobal- egg and anaemia (RBC
deficiency causes specif ic diseases. These amine) curd deficient in
compounds are called vitamins. haemoglobin)
6 Vitamin C Citrus fruits, scurvy (bleeding
Classification of Vitamins
(Ascorbic amla and gums)
Vitamins are classified into two groups depending acid) green leafy
upon their solubility in water or fat. vegetables
(i) Fat soluble vitamins:
7 Vitamin D Exposure to Rickets (bone
Vitamins which are soluble in fat and oils. But (Calciferol) sunlight, deformities in
insoluble in water are kept in this group. These are fish children) and
vitamins A, D, E and K. They are stored in liver and and egg osteo-malacia
adipose (fat storing) tissues. yolk (soft bones and
(ii) Water soluble vitamins: joint pain in
adults)
B group vitamins and vitamin C are soluble in water
so they are grouped together. Water soluble vitamins
must be supplied regularly in diet because they are
readily excreted in urine and can not be stored
(except vitamin B12) in our body.
 SOLVED EXAMPLES
Ex.1 Which of the following is not a reducing sugar- Ex.6 The simplest amino acid is-
(A) Glucose (B) Sucrose (A) Glycine (B) Alanine
(C) Mannose (D) Fructose Ans. (B) (C) Guanine (D) All the above
Sol. Sucrose is not a reducing sugar because it does Ans. (A)
not reduce fehling’s solution.
Sol. Simplest amino acid is glycine (amino acetic
Ex.2 Which one of the following is the reagent used acid H2 N– CH2 – COOH).
to identify glucose-
(A) Neutral ferric chloride Ex.7 The main structural feature of protein is–
(B) Chloroform and alcoholic KOH (A) Ester linkage (B) Ether linkage
(C) Ammonical silver nitrate (C) Peptide linkage (D) All of these
(D) Sodium ethoxide Ans. (C) Ans. (C)
Sol. Ammonical silver nitrate (Tollen’s reagent) Sol. The main structural feature of proteins is the
oxidises glucose to gluconic acid and itself presence of peptide linkage.
reduced to metallic silver.

Ex.3 Following is/are the oligosaccharides- Ex.8 The primary structure of a polypeptide is
determined by-
(A) Glucose (B) Sucrose
(A) The numer of disulphite bonds in the
(C) Lactose (D) Cellulose polypeptide
Ans. (B,C) (B) The number of amino acids in the polypeptide
Sol. Oligosaccharides are the compounds which give (C) The order of amino acids in the polypeptide
2 to 10 monosaccharides on hydrolysis. For
example - sucrose, lactose, maltose etc (D) The length of the polypeptide
Ans. (C)
Ex.4 N C  group is characteristic of - Sol. The primary structure of a polypeptide is the
| || information of order of different amino acids in
H O that polypeptide.
(A) Cellulose (B) Nucleic acid
Ex.9 DNA molecule consists of units of-
(C) Proteins (D) Phospholipids
(A) Base–sugar
Ans. (C)
(B) Base – sugar– phosphate
  N  C  (C) Base – phosphate
Sol. Peptide bond  | ||  is characteristic of
 H O  (D) None of these Ans. (B)
 
proteins. Sol. DNA has nucleotide unit, i.e., Sugar + base +
H3 PO4 .

Ex.5 The pH value of a solution in which a polar amino Ex.10 The process of formation of RNA from DNA is
acid does not migrate under the influence of known as-
electric field is called-
(A) Translation (B) Transcription
(A) Isoelectronic point
(C) Replication (D) Mutation
(B) Isoelectric point
Ans. (B)
(C) Neutralisation point
Sol. The process of formation of RNA from DNA is
(D) None Ans. (B) called transcription.
Sol. Isoelectric point is the pH at which structure of
amino acid has no charge.
Ex.11 The organic compound which will answer
Fehling’s solution test is-
(A) Ethanol (B) Acetone
(C) Maltose (D) Benzaldehyde
Ans. (C)
Sol. Maltose, being reducing sugar, reduces Fehling
solution.

Q.12 The main point of difference between DNA and

RNA is-
(A) Presence of thymine in DNA and RNA
(B) Presence of deoxyribose and thymine in
DNA, ribose and uracil in RNA
(C) Presence of ribose and thymine in DNA,
deoxybribose and uracil in RNA
(D) Presence of deoxyribose in DNA and ribose
in RNA
Ans. (B)
Sol. DNA has deoxyribose sugar, RNA has ribose
sugar with three bases common as adenine,
guanine and cytosine. DNA has fourth base
thymine ; RNA has uracil.