1.

INTRODUCTION 2
2. CARBOHYDRATES 2
3. CLASSIFICATION OF CARBOHYDRATES 2
4. PREPARATION OF GLUCOSE 3
5. DISACCHARIDES 6
6. POLY SACCHARIDES 8
7. o-AMINO ACIDS 10
8. CLASSIFICATION OF AMINO ACIDS 10
9. PROTEINS 12
10. STRUCTURE OF PROTEINS 12
11. NUCLEIC ACIDS 14
12. LIPIDS 16
CONTENTS
S.NO. TOPIC PAGE NO
1
Biomolecules
1. INTRODUCTION :
Biochemistry may be defined as the study of the chemical composition and structure of living matter
and the chemical changes that take place in them during the life processes.
Complex organic molecules (carbohydrates, lipids, proteins and nucleic acids) which govern the
common activitites of a living organism are called biomolecules.
CARBOHYDRATES :
Hydrates of carbon because the ratio of hydrogen and oxygen in these compounds is the same as
present in water.
Carbohydrates are now defined as optically active polyhydroxy aldehydes or polyhydroxy ketones
and other large molecules, like starch, glycogen or cellulose, which produce these compounds on
hydrolysis.
CLASSIFICATION OF CARBOHYDRATES :
Carbohydrates are classified into two major groups on the basis of their physical properties.
Sugars
Nonsugars or polysaccharides
Sugars
Sugars arecrystalline substances, sweet intaste, andreadilysoluble inwater. These have a fixedmolecular
weight and thus have a sharp m.p. Examples are glucose, fructose, sucrose andlactose etc.
2.
3.
(a)
(b)
(a)
Classification of carhohydrates :
BIOMOLECULES
2
Biomolecules
ONTHEBASISOFHYDROLYSIS :
Monosaccharides :
Acarbohydarte that cannot be hydrolysed further into simpler unit of polyhydroxy aldehyde or ketone
are R/a on the basis of no. of C-atoms theyare :
1.
2.
3.
4.
5.
Triose
Tetrose
Pentose
Hexose
Hebtose
Glyceraldehyde
- Crythrose
Ramnose, Ribose
- Cellulose, fructose
Rham
Oligosaccharides : Oligosaccharides are sugars which on hydrolysis give two or more molecules of
monosaccharides. These are further classified as di, tri or tetra saccharides, etc.
Disaccharides : Disaccharides are sugars which on hydrolysis produce two molecules of the same
or different monosaccharides. These are sucrose, maltose and lactose. They have the same chemical
formula C
12
H
22
O
11
.
Invertase
C
12
H
22
O
11
+ H
2
O
Sucrose

or H
+
C
6
H
12
O
6
+ C
6
H
12
O
6
Glucose Fructose

maltase
+ H
2
O C
12
H
22
O
11
Maltose
2C
6
H
12
O
6
Glucose
+
or H
Lactase
C
12
H
22
O
11
+ 2H
2
O C
6
H
11
O
6
+ C
6
H
12
O
6
or H
+
Lactose Glucose Galactose
Trisaccharides : Sugars which yield three molecules of the same or different monosaccharides on
hydrolysis are called tri-sacchardies. e.g., raffinose C
18
H
32
O
16
C
18
H
32
O
16
+ 2H
2
O
Raffinose
Polysaccharides :
C
6
H
12
O
6
+ C
6
H
12
O
6
+ C
6
H
12
O
6
Glucose Fructose Galactose
Carbohydrates whichyield large number of monosaccharides unit onhydrolysis areR/Ar polysaccharides.
4. PREPARATION OF GLUCOSE :
1. Fromsucrose :
Whensucrose is boiled with dil. HSO is alcoholic solution, to formglucose and fructose.
2 4
C H O + H O
H

+
C H O + C H O
12 22 11 2 6 12 6 6 12 6
Glucose Fructose
2. Fromstarch :
(C H
)
O + nH O
H

+
C H O
6 10 5 2 6 12 6
Glucose
n
Starch or cellulose
Chemical properties of glucose :
(i) Reaction withhydrogen Iodide, (HI).
3
Biomolecules
(ii) Reactionwith hydroxylamite
(iii) Reaction withhydrogen cyanide
(iv) reaction withbromine water.
(v) Reaction withacitic and hydride
(vi) Oxidationof glucose
The rxn indicates the presence of primary alcoholic gp. on qlucose.
STRUCTURE OF GLUCOSE :
Conjugationof monogacchazides :
Open chainstructure :
Cyanohydrin
4
Biomolecules
D& Lhas no relation with optical activity &the optical rotation in glucose molecules is given by+
Or siqn.
+ OH gp
OH gp
Hemiacetal structure
(R.H.S)
(L.H.S)
The twocyclic hemiacetal forms of glucose differ onlyinthe configuration of the hydroxyl gp at C called
1
Anomeric carbon (the aldehyde carbon before cyclisation). Such isomers i.e., o-form and
|-form, are called anomers. The six membered cyclic structure of glucose is called pyranose. Structure
because it resembele pyron ring structure.
Fructose :
Structure of fructose :
5
Biomolecules
It also exists in two cyclic forms which are obtained by the add of OHat C to the carbonyl gp. The
5
ring, thus formed, is a five membered ring and innamed as furanose.
|d() fructo furanose
Cyclic stucture of anomers of fructose :
5. DISACCHARIDES :
When asugar molecule onpeydrolysis withdilute acids, or enzymes cyield two moelcules of either
same of different monosaccharides are called disccharides.
The linkge is formed by loss of water between two monosacchocides and attached byoxygen atom
are called glcosidic linkage.
1. Sucrose :
Sucrose on hydrolysis quves equimolar mixture of D (+) Glucose and D () fructose.
Invertase
C
12
H
22
O
11
+ H
2
O
Sucrose

or H
+
C
6
H
12
O
6
+ C
6
H
12
O
6
Glucose Fructose
6
Biomolecules
The levo rotationof fructose (92.4) is more thandextrorotations fo glucose (+52.5), so the
mixture
is levorotatory.
The hydrolysis of sucrose brings a chauqe in the siqn of rotation fromdextro thus the hydrolysis of
rotation fromdextro to lawo and the product is called invert sugar.
Maltose :
2.

maltase
C
12
H
22
O
11
Maltose
+ H
2
O 2C
6
H
12
O
6
Glucose
+
or H
In C and C there is glycosidic likange. It shows reducing property so it is a reducing sugar.
1
Lactose :
4
3.
It is also R/a milk sugar as it is found inmilk.
It is composed of BDgalactose and BDGlucose.
Lactase
C
12
H
22
O
11
+ 2H
2
O C
6
H
11
O
6
+ C
6
H
12
O
6
Glucose Galactose
or H
+
Lactose
7
Biomolecules
6. POLYSACCHARIDES :
1. Starch :
It is a main storage polysaccharides of having general formula (CH O )n.
6 10 5
The main source is maize, wheat, barleyrice and potates.
It is made ofAneylose &Aneylopectin
Amylose 200 1000 zalton 10 20%
Aneylopectin 1000 500 zaltone 8085%
Amylose is made up of long - unbroanched chain of o D (+) glucose linkage.
Amylopectin is a bronched chain polymer of o D glucose units is which chain is formed by C C
1 4
qlycosidie linkage whereas branching occurs by C C qlycosidic linkage.
1 6
H
+
(C
6
H
10
O
5
)
n
+ nH
2
O
Starch
n C
6
H
12
O
6
Glucose
8
Biomolecules
2. Cellulose :
It is found incellwall of plant cells. It is a linear polymer of D C glycose inwhichqlucose units are link
together by| 1 4 glycosidic linkage.
It is a non-reducing sugar.
Relative sweetness of sugar
Sugar Relative
sweetness
100 (standard) Glucose
16 Invertsugar
32 Fructose
33
Sugar Relative
sweetness
74
130
173
Sucrose
Lactose
Galactose
Maltose
Cellulose is the most important natural polymer whose chemical treatment gives various useful
derivatives e.g.,
a.
b.
Rayon : Cellulose acetate and cellulose xanthate are used as a fibre.
Celluloid : Cellulose dinitrate also known as pyroxylin, mixed with plasticizer and alcohol,
is used for the manufacturing of photographic film, spectacle frames, piano keys, etc. It is
known as artificial ivory.
Explosive : Cellulose trinitrate is used extensively as a blasting and propellant explosive.
Lacquer: Collodion is used for manufacturing washable cellulose paints.
Water proofing : Solution of cellulose acetate is used to provide antishrink property to textile
fabric.
Methyl cellulose is used in fabric sizing, paste and cosmetics. Ethyl cellulose is used for
manufacturing of rain coats and plastic films.
c.
d.
e.
f.
S.No. Amylose Amylopectin
1. It is water soluble fraction of starch It is water insoluble fraction of starch.
2. It is 20% of the quantity of starch It is 80% of starch.
3. It is a straight chain polymer of
D-glucose units.
It is branched chain polymer of
D-glucose units.
4.
In amylose, the glucose units are joined
by o-1, 4 glycosidic linkage
In amylopectin, the glucose units are
joined by o-1, 6 glycosidic linkage.
5. Its molecular mass lies in the range of
10,000 50,000
Its molecular mass is in the range of
50,000 1,00,000.
9
Biomolecules
7. o-AMINO ACIDS :
o-Amino acids are substituted carboxylic acids in which one o-hydrogen atoms of alkyl group is
substituted by amino (NH
2
) group. These may be represented by the general formula.
o
where R = H or alkyl group
R CH COOH
NH
2
Structure of o-amino acids
The amino acids containing one carboxylic group and one amino group behave like a neutral molecule.
This is due to the fact that in aqueous solution the acidic carboxylic group and basic-amino group
neutralise each other intramolecularly to form an internal salt structure, known as zwitter ion or
dipolar ions.
+
NH
2
R C COOH
NH
3
R CH COO

Zwitter ion
However, the neutral zwitter ion (dipolar ions) changes to cation in acidic solution and exist as anion
in alkaline medium. Thus amino acids exhibit amphoteric character.
Alkali
Acid
H
2
N CH COO

H
3
N
+
CH COO

H
3
N
+
CH COOH
R
Zwitter ion
R R
Cation Anion
Therefore, amino acid exist as zwitter ion when the solution is neutral or its pH ~ 7. The pH at which
the structure of an amino acid has no net charge is called its isoelectric point.
8. CLASSIFICATION OFAMINO ACIDS :
o-Amino acids are broadly classified in three main groups based on the relative number of NH
2
and
COOH group
(i) Neutral amino acids : Amino acids containing one NH
2
group and one COOH group
are called neutral amino acids e.g., glycine, valine, alanine, etc.
(ii) Basic amino acids: Amino acids which contain one COOH group and two NH
2
groups
are called basic amino acids e.g., lysine and arginine.
(iii) Acidic amino acids : Amino acids containing two COOH groups and one NH
2
group are
classified as acidic amino acids e.g., aspartic acid and glutamic acid, etc.
10
Biomolecules
List of 20 naturally occuring o-amono acids.
o-Amino acid
Abbreviation
or code
Structure
NEUTRAL
Glycine Gly H
2
N CH
2
COOH
H
2
N CH COOH
1.
2.
Alanine Ala
CH
3
3.
Valine Val H
2
N CH COOH
CH (CH
3
)
2
4. Proline Pro
Asp
ACIDIC
5. Serine Ser H
2
N CH COOH
CH
2
OH
H
2
N CH COOH 6. Aspartic acid
CH
2
COOH
H
2
N CH COOH 7. Glutamic acid Glu
CH
2
CH
2
COOH
BASIC
8. Lysine* Lys H
2
N CH COOH
CH
2
CH
2
CH
2
CH
2
NH
2
H
2
N CH COOH
CH
2
(CH
2
)
2
NH C NH
2
9. Arginine* Arg
NH
11
Biomolecules
9. PROTEINS :
Proteins are complex, nitrogeneous organic substance which occur in all animals and plants. They are
so named because proteins are the most vital chemical substances of primary importance neccessary
for the normal growth and maintenance of life. Protein serves following functions in our body.
a.
b.
c.
d.
e.
To promote growth.
To supply essential amino acids to blood.
To maintain body tissues.
To synthesize various enzymes.
To protect body from infection.
Protein content of food stuffs
Food stuff % Protein Food stuff % Protein
Milk
Wheat
Peas
Maize
5
14
21
10
Meat 24 26
Egg yolk
Egg (white)
Cheese 33
16
12.5
Classification of proteins
Proteins are classified by two different methods. According to first mode of classification proteins are
of two types depending upon their shape and functions.
(a)
(a)
Fibrous proteins (b) Globular proteins
Fibrous proteins : These have thread like molecules which lie side by side to form fibres.
The various molecules are held together by hydrogen bonds. These are insoluble in water but soluble
in concentrated acids and alkalis e.g., hair, nails, wood, feathers and horn, etc, are made up of
keratin. Muscles have myosin. Silk is composed of fibroin. Bones and cartilage have collagen.
(b) Globular proteins : This type of protein has molecule folded into compact units which often
acquire spheroidal shape. Such proteins are soluble in water, dilute acids and alkalis e.g., insulin,
hemoglobin, albumin, etc.
STRUCTURE OF PROTEINS :
The structure of proteins is quite complex. Study of its structure is carried out under the following
headings.
10.
(a) Primary structure of protein : The primary structure of protein refers to its covalent
structure, i.e., the sequence in which various o-amino acid are arranged in protein or in the
polypeptide structure of protein.
The linkage CO NH is known as peptide linkage.
H
2
N CH COOH + H
2
N CH COOH
R
R'
CH COOH + H
2
O H
2
N CH
Peptide bond
R
R'
The dipeptide still has free amino and carboxyl groups through which it an react with other molecules
of amino acid resulting in polypeptide formation
R' O O
C
H H
N
R'''
CH N CH C
CH CH C N C N
R O
C-terminal
R
R'' O H
N-terminal
Linear polypeptide chain
CONH
12
Biomolecules
In polypeptide chain, the free amino end is termed as N-terminal and the free carboxyl end is said
to be C-terminal end.
Secondary structure of proteins
Secondary structure of protein refers to the arrangement of polypeptide chains into a definite three
dimensional structure which protein assumes as a result of hydrogen bonding. Depending upon the
size of the R-group of the amino acids in polypeptides, two different types of secondary structure are
possible as discussed below
(a) o-helix structure (b) |-Pleated structure
o-Helix structure : This type of secondary structure is acquired when the R groups in amino acids
are large and involve in coiling of the polypeptide chains. The helical pattern in right handed coil and
the shape is stabilised by the intra molecular hydrogen bond bet ween t he
>C = O group of one amino acid and NH group of the fourth amino acid.
|-Pleated structure : This type of secondary structure is acquired when the R groups of amino acids
are small. In this structure the linear polypepotide chains are arranged side by side and held together
by intermolecular hydrogen bond between the C = O and NH group.
R O H
N
H
R
H
C C C
C
O
C
O
N C N
H
H
R
H
O
H
H
O H R
N
C C
C N
C N C C
H H R
R
O
H
7.2
Tertiary structure of proteins
The tertiary structure of protein is the most stable shape that a protein assumes under the normal
conditions of temperature and pH. During acquiring of tertiary structure, various types of attractive
forces between the amino acid chains are involved. These attractive forces, like hydrogen bond,
disulphide bonds, ionic, chemical and hydrophobic bonds, result in a complex and compact structure
of protein. The two important teritary structures of proteins are fibrous structures and globular
structure. Fribrous proteins have largely helical structure and are rigid molecules of rod like shape.
Globular proteins, on the other hand, have a polypeptide chain which consist partly of helical sections
and partly |-pleated structure and remaining in random coil form. These different segment of
secondary structure then fold up to give protein a spherical shape.
13
Biomolecules
Quaternary structure of proteins
The quaternary structure of protein is developed when the polypeptide chains, which may or may not
be identical are held together by hydrogen bonds. It results in the increase of molecular mass of
protein greater than 50,000 amu. For example, haemoglobin contains four submits, two identical o-
chains containing 141 amino acids each and the other two identical |-chains containing 161 amino
acids each.
Denaturation of proteins
When the proteins are subjected to the action of heat, mineral acids or alkali, the water soluble form
of globular protein changes to water insoluble fibrous protein resulting in the precipitation or
coagulation of protein. This is called denaturation of proteins.
11. NUCLEIC ACIDS :
Nucleic acids are vital biomolecules which are present in the nuclei of all living cells in the form of
nucleoproteins. These are long chain polymers with a high molecular mass. These are also known as
biopolymer having nucleotide as a repeating structural unit (monomer). These play an essential role
in transmission of the heredity characteristics from one generation to the next and also in the
biosynthesis of proteins. Therefore, the genetic information coded in nucleic acid governs the structure
of protein during its biosynthesis and hence controls the metabolism in the living system.
The nucleic acids are of two types differing mainly in the nature of carbohydrate present in them.
(i)
(ii)
Structure
DNA(Deoxyribonucleic acid)
RNA(Ribonucleic acid)
of nucleic acids
The nucleic acids are the posthetic component of the nucleoproteins. Nucleic acid on stepwise
hydrolysis gives following products as shown in the chart
Nucleic acid
Hydrolysis
Nucleotides
Hydrolysis
Phosphoric acid
Nucleosides
Hydrolysis
Pyrimidine bases
(Thymine and cytosine) fromDNA
(Uracil and cytosine) fromRNA
Purine bases
(Adenine and guanine)
Pentose sugar
Ribose or
Deoxyribose
14
Biomolecules
Difference between DNA and RNA
The main points of difference betwen the two types of nucleic acids are given in the table.]
Ribonucleic acids
1.
2.
The pentose sugar in RNAis ribose.
Purine bases of RNAare represented by adenine and guanine, the pyrimidine bases are uracil and
cytosine.
The thymine inDNAis replaced byuracil in RNA.
RNAis single stranded, but double stranded RNAis present in Rheovirus and wound tumour virus.
There are three major classes of RNA, each with specific functions in protein synthesis
3.
4.
5.
mRNA
6.
7.
8.
tRNA
9.
10.
11.
12.
Messenger RNAis produced by DNA; the process is called transcription.
Messenger RNAencodes the amino acid sequence of a protein in their nucleotide base sequence.
Atriplet of nitrogenous bases specifying an amino acid in mRNAis called codon.
tRNAis also known as soluble RNA(sRNA) it is soluble in 1 molar solutionof sodiumchloride.
tRNAidentifies amino acids in the cytoplasmand transports themto the ribosome.
Molecules of tRNAare single-stranded and relativelyverysmall.
Anticodon is a three-base sequence in a tRNAmolecule that forms complementary base pairs with a
codon of mRNA.
All transfer RNApossess the sequence CCAat their 3' ends; the amino acid is attached to the terminal
Aresidue.
13.
rRNA
14. Ribosomal RNAis found in ribosomes of cells and is also called insoluble RNA.
DNA RNA
1.
2.
3.
4.
5.
6.
7.
The pentose sugar present in it is 2-
deoxy D() ribose.
It contains cytosine and thymine as
pyrimidine bases
DNA is double strand and pairing of
bases is present throughout the
molecule.
It occurs in the nucleus of the cell.
It is a very large molecule and the
molecular weight vary from 6 million to
16 million amu.
It has a characteristic property of
replication
DNA controls the heredity character.
It has D () ribose sugar.
It contains cytosine and uracil as
pyrimidine bases.
It is a single strand molecule looped
back on itself. The pairing of bases is
present only in helical part.
It mainly occurs in the cytoplasm of the
cell.
It is a much smaller molecule and its
molecular weight ranges from 20
thousand to 40 thousand.
It does not replicate.
RNA only governs the biosynthesis of
proteins.
15
Biomolecules
15. The mainfunctionof rRNAis to attract andprovide large surface for spreading oom-RNAover ribosomes
during translocation process of protein synthesis.
Type SedimentationMol. Wt.
coefficient
Number of
nucleiotide residues
75-3000
75-90
100
1500
3100
% of total cell
RNA
2
16
mRNA
tRNA
rRNA
6 to 25S
4S
5S
16S
23S
25,000-1000,000
23,000-30,000
35,000
550,000
1100,000
82
Genetic Code
16. The relationship between the sequence of amino acids in polypeptide with base sequence of DNAor
mRNAis genetic code.
Genetic code determines the sequence of amino acids in a protein.
Atriplet would code for a given amino acid as long as three bases are present in a particular sequence.
Later in a cell-free system, Marshall Nirenberg and Philip Leder (1964) were able to showthat GUU
codes for the amino acid valine.
The spellings of further codons were discovered by R. Holley, H. Khorana and M. Nirenberg. They
have been awarded the Nobel Prize in 1968 for researches in genetic code.
LIPIDS
The term lipids represent a group of biomolecules which are insoluble in water but soluble
in organic solvents of low polarity such as chloroform, toluene, ether, carbon tetrachloride,.
They also serve as the energy reserve for living cells.
Lipids are classified in three groups
17.
18.
19.
20.
12.
(i)
(ii)
(iii)
Triglyceride esters of higher fatty acids or oils and fats
Phospholipids
Waxes
16
Biomolecules
Ex.1 Glucose or sucrose are souble in water but cyclohexane or benzene (simple six membered ring com-
pound) are insoluble inwater. Explain.
Glucose contains five OHgroups and sucrose contains eiht OHgroups formhydrogen-bonds with
water. Because of this extensive intermolecuar Hydrogen-bonding, glucose and sucrose are solublke in
water irrespective of the fact that their molecular masses are 180 amu and342 amu respectively.
Onthe other hand, benzene (molecular mass = 78) and cyclohexane (molecular mass =84) are simple
molecular having lowmolecular masses. Even then theyare insoluble in water. The reason being that
these compounds do not contain OHgroups and hence do not formhydrogen-bonds with water.
What products are expected when lactose is hydrolysed ?
On hydrolysis, loctose gives two molecules of monosaccharides, i.e., onle molecule of D-(+)- glucose
and D-(+)-Galactose.
Sol.
Ex.2
Sol.
+
H
3
O
+ H
2
O C
12
H
12
O
11
Lactose
C
6
H
12
O
6
C
6
H
12
O
6
+
or Lactase
D(+)Glu cos e D(+)Galactose
Ex.3
Sol.
Ex.4
Sol.
What the constituents of maltose.
It is a polysaccharide. It is polymer of D-glucose. It stores food in animals and human beings.
What are polysaccharides ? Give one example ?
Polysaccharides are thecarbohydrates which on hydrolysis give a large number of molecules of monosac-
charides. For example, starch or cellulose.
What is difference between amylose and amylopectin.
Amylose is water soluble linear of a-glucose. Amylopectin is water insoluble brancehd chain polymer of
o-glucose.
What are oligosaccharides ?
Carbohydrates which onhydrolysis give 2-10 molecules of monosaccharides are called oligosaccha-
rides. For example, sucrose, raffinose, stachyrose, etc.
What is mutarotion ?
The spontaneous change of specific rotation of anopticallyactive substance with time is called mutaro-
tation.
What are amino acids ?
Amino acids are biomolecules which contain amino (NH ) group at o-carbon and a carboxylic acid
Ex.5
Sol.
Ex.6
Sol.
Ex.7
Sol.
Ex.8
Sol.
2
group (COOH).
Howdo you explain the absence of aldehyde group in pentaacetate of glucose ?
The cyclic hemicetal formof glucose contains an OHgroup at C-1 which gets hydrolysed inthe queous
solution to produce the open chain aldehydic formwhich thenreacts with NH OHto formthe corre-
Ex.9
Sol.
2
sponding oxime. Therefore, glucose contains an aldehydic group. On the other hand, when glucose is
reacted with acetic anhydride, the OHgroup at C-1, along withthe four other OHgroups at C-2, C-3,
SOLVEDEXAMPLE
17
Biomolecules
C-4 and C-6forma pentaacetate. As the pentaacetate of glucose does not contain a free OHgroup at
C-1, it cannot get hydrolysed inaqueous solution to produce the open chain aldehydic formand thus
glucose pentaacetate does not react withNH OHto formglucose oxime.
2
Hence, glucose pentaacetate does not contain the aldehyde groups.
State two mainfunctions of carbohydrates ?
(i) Carbohydrates act as biofuel to provide energy for functioning of living organisms.
Ex.10
Sol.
(ii) Theyact as constituents of cell walls.
Ex.11
Sol.
What is the structural feature characterising reducing sugars ?
The main structural feature of reducing sugar is the presence of analodehyde group ( CHO) suchasin
glucose, mannose galactose, etc. or o-ketol grouping (COCH OH) as present in fructose.
2
Ex.12
Sol.
Ex.13
Sol.
Ex.14
Sol.
Ex.15
Sol.
What is invert sugar ?
An equimolar mixture of glucose and fructose is called invert sugar.
What are constituent units of cellulose ?
Cellulose is a linear polymer made upof D(+) glucose molecules linked by|-glycosidec bonds.
Why is cellulose not digested inhuman body ?
It is due to the fact that humajhn beings do not have enzyme to digest cellulose.
What is meant byinversion of sugar ?
Sucrose is dextrorotatory but on hydrolysis, it gives an euimolar mixture of D(+)-glucose and D()-
fructose which is levorotatroy. This cange of specific rotation fromdextrorotation to laevorotationis
known as inversion of sugar.
18
Biomolecules
Ex.16 The meltaing points and slubilityin water of amino acids are higher thanthose of the correspondinghalo
acids. Explain.
+
Sol. The amino acids exist as zwitter ions,

. Because of this dipolar salt like charactor,
H
3
N OHR COO
theyhave strong dipole-dipole attractions. So, their melting points are higher than halo acids which do
not have salt like character. Moreover, due to this salt like character, they interact strongly withH O.
2
Thus solubilityinwater of amino acids is higher than that of the corresponding halo acids which donot
have salt like character.
Where does the present in the egg go after boiling the egg ?
On boiling the egg, the proteins under go denaturation and the water present inthe egggets absorbed or
adosorbed inthe denaturated proteins probablythrough H-bonding.
Explain whyvitamin Ccan not be stored in the body ?
Vitamin Cis soluble inwater, hence, it is readilyexcreted inurine andthus cannot be storedin the body.
What products would be formed when a nucleotide from DNA containing thymine is
hydrolysed ?
Besides thymine, the two products are 2-deoxy-D-ribose and phosphoric acid.
When RNAis hydrolysed, there is no relationship among the quantities of different bases obtained ?
What does this fact suggest about the structure of RNA?
ADNAmolecule has two strands in which the four complementary bases pair each other, viz. cytosine
(C) always pairs with guanine (G) while thymine (T) always pairs with adenine (A). Therefore, when a
DNAmolecule is hydrolysed, the molar amounts of cytosine is always equal to that of guanine and that
of adenine is always equal to that of thymine. RNAalso contains four bases, the first three are same as
in DNAbut the fourthone is uracil (U)
As in RNAthere is no relations hip between the quantities of four bases (C, G, Aand U) obtained,
therefore, tthe base-pairing principle, viz. a pairs with Uand Cpairs withGis not followed. So unlike
DNA, RNAhas a single strand.
Ex.17
Sol.
Ex.18
Sol.
Ex.19
Sol.
Ex.20
Sol.
19
Biomolecules
Q.1 What happens whenD-glucose is treated with
the followingreagents?
Q.18 (a) Give reasons for the followingstatements :
(i)Amino acids are amphoteric in nature .
(ii) Amino acids have comparatively higher
melting po ints than the corr esponding
haloacids.
(b) What deficiency diseases are caused due
to lack to lack of vitamins A, B , B and Kin
(i) HI (ii) Bromine water (iii) HNO
3
Q.2 Define the following terms in relation to
proteins
(i) Peptide linkage (ii) Denaturation.
1 6
Q.3 Define the following as related to proteins
human diet?
(i) Peptide linkage
(iii) Denaturation.
(ii) Primarystructure
Q.19 The twostrands in DNAare not identical but
are complementary. Explain.
State difference betweenthe following pair
(i) o-helix and |-pleated structures.
(ii) Primary and secondary structures of a
protein.
What are nucleic acids? Mention their two
important functions.
What is the difference between a nucleoside
and a nucleotide?
What are reducing and non-reducing sugars ?
What is the structural feature characterising
reducing sugars ?
Distinguishbetweeno-glucose and|-glucose.
What happens when D-glucose treated with
the following reagents ?
Q.4 What are the common types of secondary
structure of proteins?
Howdo you explain the amphoteric
behaviour of amino acids?
What is the effect of denaturation on the
structure of proteins?
Describe the following
Q.20
Q.5
Q.6
Q.21
Q.7
Q.22
(i) Glycosidic linkage (ii) Peptide linkage
Q.8 Enumerate the reactions of D-glucose which
cannot be explained by its open chain
structure.
What are essential and non-essential amino
acids? Give two examples of each type.
List any for vitamins. Mention the chief sources
and functions of two of them.
(i) What are essential and non-essential amino
acids ? Give two examples of each.
(ii) What is a denatured protein
How are vitamins classified? Name the vita-
min responsible for the coagulation of blood.
Why are vitamin A and vitamin C essential to
us? Give their important sources.
Draw open chain structure of aldopentose and
aldohexose. Howmany asymmetric carbons are
present in each ?
(a) Describe the following giving one example:
Nucleotides.
(b) List four functions of carbohydrates in living
organisms.
What type of bonding helps in stabilising the
Aohelix structure of proteins?
Differentiate between globular and fibrous
proteins.
Q.23
Q.9
Q.24
Q.25
Q.10
(i) HI (ii) Bromine water (iii) HNO
3
Q.26 Write the important structural and functional
differences between DNAand RNA.
What are the different types of RNAfound in
the cell ?
Define the following and give one example of
each
Q.11
Q.27
Q.12
Q.28
Q.13
(a) Isoelectric point
(c) Enzymes.
(b) Mutarotation
Q.14
Q.29 Answer the following queries about proteins ?
(i) Howare proteins related to amino acid ?
(ii) How are oligopeptides different from
polypeptides ?
(iii) Whenis a protein said to be denatured ?
(a) Name the three major classes of carbohy-
drates and give the distinctive characteristic of
each class.
(b) What are nucleotides ? Name two classes
of nitrogen containing bases found amongst
nucleotides.
Q.15
Q.30
Q.16
Q.17
EXERCISE-I
20
Biomolecules
Q.1 State a use for the enzyme streptokinase in
medicine.
Describe the following :
(i) Denaturationof Proteins
Differentiate between:
Primary structure and secondary structure of
proteins
Why is cellulose in our diet not nourishing ?
Write the major classes in which t he
carbohydrates are divided depending upon
whether these undergo hydrolysis, and if so,
on the number of products formed.
Explain mutarotation taking D-glucose as an
example.
Enumerate the structural difference between
DNA and RNA. Write down the structure of
sugar present in DNA.
(a) Answer the following queries about pro-
teins
(i) How are proteins related to amino acids ?
(ii) How are oligopeptides different from
polypeptides ?
(iii) Whenis a protein said to be denatured ?
(a) Define and classify vitamins. Give at least
two examples of each type.
(b) Define enzymes and comment on the
specificity in action of an enzyme. Illustrate with
an example.
What are essential an non-essential amino
acids ? Give two examples of each.
(a) Define the following terms:
(i) Co-enzymes
(ii) Nucleotides
(b) List four main functions of carbohydrates
inorganisms.
(a)Answer the following questions briefly
(i) What areanytwo goodsourcesofvitaminA?
(ii) What are nucleotides ?
(b) Howare carbohydrates classified ?
Write two main functions of carbohydrates in
plants.
What happens whenD-glucose is treated with
the following reagents ?
Q.16 Name two fat soluble vitamins, that sources
and diseases caused due to their deficiency in
diet.
State a use for the enzyme streptokinase in
medicine.
Describe the following :
Denaturationof Proteins
Differentiate between:
Primary structure and secondary structure of
proteins
Whyis cellulose inour diet not nourishing ?
Writ e t he major classes in which the
carbohydrates are divided depending upon
whether these undergo
Aspartame, an artificial sweetener, is a peptide
and has the following structures :
Q.2
Q.17
Q.3
Q.18
Q.4
Q.5
Q.19
Q.20
Q.21
Q.6
Q.7
Q.22
Q.8
NH
2
CH C H
2 6 5
HOOC CH
2
CH CONH CH COOCH
3
(a) Identify the four functional groups.
(b) Write the zwitterionic structure
(c) Write the structures of the amino acids
obtained from the hydrolysis of aspartame.
(d) Which of the two amino acids is more
hydrophobic ?
Give the chemical name of vitamin B .
Q.9
Q.23
Q.24
12
Q.10
What are the following substances ?
(i) Invert sugar (ii) Polypeptides
Which forces are responsile for the stabilityof
o-helix ? Whyis it named as 3.6 helix ?
Q.11
Q.25
13
What are complementary bases ? Draw
structure to showhydrogen bonding between
adenine and thymine and between guanine and
cytosine.
Give reasons for the following :
(i) On electrolysis in acidic solution amino ac-
ids migrate towards cathode, while in alkaline
solution these migrate towards anode.
(ii) The monoaminomonocarboxylic acids have
two pKvalues.
Glycine exists as a Zwitter ion but anthranilic
acid does not. Comment.
Write the difference between DNA and RNA ?
Explain structure of protin ?
Q.26
Q.12
Q.27
Q.13
Q.14
Q.28
(i) alk.KMnO (ii) Br + CS (iii) H SO
4 2 2 2 4
Q.29
Q.30
Q.15 Name the four bases present in DNA. Which
one of these is not present in RNA?
EXERCISE-II
21
Biomolecules
Q.1
The chromophore in the dye
Q.9 Peptide bond is
(a) CO NH
(b) NH CO NH R
HO
3
S
N = N N(CH
3
)
2
(b) SO
3
H
(d) N = N
is
2
(c) R CO NH R
(d) CONH
2
During hydrogenation of oils, higher melting
vegetable ghee is formed because
(a) Hydrogen is dissolved in the oil
(b) Hydrogen combines with oxygen of the oil
(c) Esters of unsaturated fattyacids are reduced
to those of saturated acids
(d) Hydrogen drives off the impurities fromthe
oil
Structurally a biodegrable detergent should
contain a
(a) Normal alkyl chain
(b) Branched alkyl chain
(c) Phenyl side chain
(d) Cyclohexyl side chain
Which of the following dye has a nitro group ?
(a) N(CH
3
)
2
(c) C
6
H
5
Q.10
Q.2 At the isoelectric point for an amino acid the
species present are
(a) RCHCOOH
|
NH
2
(c) RCHCOO

|
NH
2
(b) RCHCOOH
|
+
NH
3
(d) RCHCOO

|
+
NH
3
Q.11
Q.3 Secondarystructure of a protein refers to
(a) Mainly denatured proteins and structures
of prosthetic groups
(b) Regular folding patterns of contiguous
portions of the polypeptide chain
(c) Linear sequence of amino acide residues in
the polypeptide chain
(d) None of these
The general formula of carbohydrates is:
(a) C H O
Q.12
(a) Malachite
(c)Aniline yellow
(b) Indigo
(d) Martius yellow
Q.4
Q.13 Glucose and Fructose are
(a) Tautomers
(b) Chain isomers
(c) Functional isomers
(d) Geometrical isomers
Glucose is
n 2n+1
(b) C H O
n 2n
(c) C (H O) or C (H O)
n 2 n x 2 y
(d) C (H O)
n 2 2n
Q.5 Which of the following is a disaccharide?
Q.14
(a) Sucrose
(c) Fructose
(b) Glucose
(d) Starch
(a)Aldopentose
(c) Ketopentose
(b)Aldohexose
(d) Ketohexose
Q.6 The ironinhaemoglobin is bound by Q.15 Asubstance whichcanact bothas anantiseptic
and disinfectant is (a) Hydrogen bonds
(c) Ionic bonds
(b) Chelation
(d) Covalent bonds (a)Aspirin
(c) Bithional
(b) Chloroxylenol
(d) Phenol
Q.7 Whichofthefollowingstatement(s) is(are) true?
(a)All amino acids contain one chiral center
(b) Some amino acids containone, while some
contain more chiral center or even no chiral
center
(c) All amino acids found in proteins have L
configuration
(d) All amino acids found in proteins have 1
amino group
Anomers have different
Q.16 Thrust imparted to the rocket is governed by
the
(a) Thirdlawof thermodynamics
(b) Gravitational law
(c) Newtons third law
(d) None of these
Which of the following represent a bi-liquid
propellant?
(a) N
2
O
4
+unsymmetrical dimethylhydrazine
(b) N
2
O
4
+ acrylic rubber
(c) Nitroglycerine +nitrocellulose
(d) Polybutandiene +ammoniumperchlorate
Q.17
Q.8
(a) properties
(c) specific rotation
(b) melting points
(d) all of these
EXERCISE-III
22
Biomolecules
Choose the correct relationship for o-D-
glucose (1) and |-D-glucose(2)
(a)Aand Bare epimers
(b)Aand Bare crystal modification
(c) Ais a pyranose sugar and B is furanose
sugar
(d)Ais an aldose and Bis a ketose.
Natural rubber is a polymer of
Q.18 The reagent usedinRuffs degradation is Q.26
(a) Baeyers reagent
(c) Fentons reagent
(b) Tollens reagent
(d) Benedicts reagent
If K and K are theionization constants of Q.19
a
1
a
2
H N
+
CHICOOH and H N
+
CHICOO

, re-
3 3
spectively, the pHof the solution at the iso-
electric point is
Q.27
pH = pK + pK (a) (a) Chloroprene
(c) 1,3-Butadiene
(b) Isoprene
(d) None
a
1
a
2
1/ 2
(b) pH = (pK
a
+ pK
a
)
1 2
Q.28 Hydrolysis of sucrose is called
1/ 2
(c) pH = (pK
a
+ pK
a
)
1 2
(a) Saponification
(c) Esterification
(b) Inversion
(d) Hydration
(pK
a
+ pK
a
)
pH = (d)
1 2
Q.29 Glucose and fructose give the same osazone.
One may, therefore, conclude that
(a) Glucose and fructose have identical
structures
(b) Glucose and fructose are anomers
(c) Thestructures of glucose andfructose have
mirror-image relationship
(d) The structures of glucose andfructose differ
only in those carbon atoms which take part in
osazone formation.
In vulcanization of rubber
(a) Sulphur reacts to forma newcompound
(b) Sulphur cross-links are introduced
(c) Sulphur forms a very thin protective layer
over rubber
(d)All statements are correct
The simplest amino acid is
2
Q.20 Placedo is oftengiven to patients. It is
(a) an antidepressant
(b) a broad spectrumantibiotic
(c) a sugar pill
(d) a tonic
Coordination polymerization was developed
by
Q.21
(a) Zeigler and Natta
(c) Beckmann
(b) Linus Pauling
(d) None of these
Q.30
Q.22 Teflon, polystyrene andneoprene are all
(a) Copolymers
(b) Condensation polymers
(c) Homopolymers
(d) Monomers
Carbohydrates whichdiffer inconfiguration at
the glycosidic carbon (i.e. C inaldose and C
Q.31
Q.23
(a) glycine
(c) guanine
(b) alanine
(d) all of the above
1 2
in ketoses) are called
(a)Anomers
(c) Diastereomers
An aldohexose
(b) Epimers
(d) Enantiomers
(e. g. ,glucose) and
Q.32 Which of the following belong to the class of
natural polymers?
(a) Proteins
(c) Rubber
(b) Cellulose
(d)All of the above
Q.24
2-oxohexose (e.g. , fruct ose) can be
distinguished withthe help of
Q.33 Pick out correct statements.
(a) In an electrolysis experiment, amino acids
migrate at the isoelectric point towards
electrodes
(b) p-aminobenzenesulphonic acid is a dipolar
ion: while p-aminobenzoic acid is not
(c) Sulphanilic acid is soluble in base, but not
inacid
(d) H
3
NCH
2
COOH(pka = 2.4) is more acidic
than RCH
2
COOH(pK
a
= 4 5)
(a) Tollens reagent
(c) Benedict solution
(b) Fehlings solution
(d) Br
2
/ H
2
O
Q.25 The open-chain glucose on oxidation with
HIO
4
gives
(a) 5 HCOOH + H
2
C = O
(b) 4 HCOOH + 2 H
2
C = O
(c) 3 HCOOH + 3 H
2
C = O
(d) 2 HCOOH + 4 H
2
C = O
+
23
Biomolecules
o-D-Glucose and |-D Glucose differ from
each other due to difference inone of carbon
with respect to its
(a) Size of hemiacetal ring
(b) Number ofOH groups
(c) Configuration
(d) Conformation
For oamino acid having the structure
RCHCO
2
H
Q.34 Q.42 Glucose molecule reacts with X number of
molecules of phenylhydrazine to yield osazone.
The value of Xis
(a) Three
(c) One
(b) Two
(d) Four
Q.43 Mainstructural unit of protein is
(a) Ester linkage
(c) Peptide linkage
(b) Ether linkage
(d)All the above
Q.35
Q.44 Which of the following statements is true of
proteins?
(a) Theycatalyse the biochemical reactions
(b) Theyact as antibodies
(c) Theyact as hormones
(d) Theyperformall these functions
Which of the following is a polysaccharide ?
|
NH
2
Which of the following statements are true?
(A) Water solubilityis maximumat a pHwhen
concentration of anions and cations are equal.
(B) Theygive ninhydrin test
(C) On reacting with nitrous acid give off N
2
Q.45
(a) Glucose
(c) sucrose
(b) Galactose
(d) Pectines.
(a)All
(c) Aand B
(b) B and C
(d) None of these
Q.46 Starch can be used as an indicator for the
detection of traces of
(a) Glucose inaqueous solution
(b) Proteins in blood
(c) Iodine inaqueous solution
(d) Urea in blood
Whichof thefollowingstatements about ribose
in incorrect ?
(a) It is a polyhydroxy compound
(b) It is an aldehyde sugar
(c) It has six carbon atoms
(d) It exhibits optical activity
The letter Dincarbohydrates represents
Q.36 Glucose gives the silver mirror test with
ammoniacal solutionofsilver nitrate because it
contains
(aAldehydes group
(c) Ketone group
(b) Ester group
(d)Amide group
Q.37 Oligosaccharides contain .
sugar units
Simple
Q.47
(a) 2 to 10
(c) 6 to 12
(b) 4 to 8
(d) 6 to 10
Q.38 Apair of diastereomers that differ only in the
configuration about a single carbon atomare
called
Q.48
(a)Anomers
(c) Conformers
(b) Epimers
(d) Enantiomers
(a) It direct synthesis
(c) Its mutarotation
(b) Its dextrorotation
(d) Its configuration
Q.39 Pick out the incorrect statement aboutATP.
(a) It is a nucleotide
(b) It contains the purine, adenine
(c) The enzyme-catalysed hydrolysis of ATP
t o ADP and AMP is accompanied by
absorption of energy
(d) Energy is stored in the cell in the formof
ATP.
If the sequence of bases in one strand of DNA
is ATGACTGTC, then the sequence of bases
in its complementary strand is
Q.49 Which of the following is the structure of
D-xylose?
CHO
CHO
HO
HO
(b) H
H
H
OH
HO
H
H
H
OH
OH
(a)
CH OH
CH
2
OH
CHO
2
CHO
H
H
(d)
OH
OH
OH
Q.40 H
HO
(c)
OH
H
OH H
H
CH
2
OH
CH
2
OH
(a) TACTGACAG
(c) GUAGTUAUG
(b) TUCTGUCUG
(d) None of these
Q.50 Glucose gives the silver mirror test with
ammoniacal solutionofsilver nitrate because it
contains the group
Q.41 Cellulose is a linear polymer of
(a) o-glucose
(c) o-fructose
(b) |-glucose
(d) none of these
(a)Aldehyde
(c) Ketone
(b) Ester
(d)Amide
24
Biomolecules
Comprehension :
Dye is a natural or synthetic colouring matter
which is used in solution to stain materials
especially fibres. All the coloured substances
are not dyes. Acoloured substance is termed
as a dye if it fulfills the following conditions.
(a) It must have a suitable colour.
(b) It can be fixed on the fibre directly or
which the help of a mordant.
(c) When fixed, it must be fast to light and
washing.
According to the modern theory.
(a) It must have a chromophoric group.
(b) It must have certain groups which themself
donot produce colour but when present with
chromophore, it intensifies the colour.
(a) If bothAand Rare trueandRisthe correct
explanationof A.
(b) If both Aand R are true but R is not the
correct explanationof A.
(c) If Ais true but Ris fals.
(d) If both Aand Rare false.
A. The enzyme amylase hydrolyses starch to
maltose.
R. Starch is polymer containing glycosidic
linkages.
A. During emergency, hormone adrenaline
stimulates the conversionof liver glycogen into
glucose.
R. Adrenaline is an example of peptide
hormone.
A. A so lut io n o f su cr o se in wat er is
dextrorotatorybut onhydrolysis inthepresence
of small amount of dil. HCl, it becomes
laevorotatory.
R. Sucrose on hydrolysis gives unequal
amounts of glucose and fructose as a result of
whichchange in sign of rotationis observed.
A. Each turnof the a-helix structure of protein
forms o13 membered ring is containing 3.6
amino acids.
R. o-helix is secondary structure of protein
which gets stabilised via hydrogenbondingand
disulphide linkages.
A. o-glucose and b-glucose are the anomers
of glucose having different specific optical
rotation.
Q.54
Q.55
Q.56
Q.51 The groups which by themselves do not
produce colour but intensify the colour when
present with the chromophores are called.
(a) substituents
(c) cataphores
(b) auxochromes
(d) chromogens
Q.52 Which of the following is an anthraquinone
dye? Q.57
(a) phenolphthalein
(c) malachite green
(b) congo red
(d) alizarin
Q.53 Alizarin gives violet colour with which of the
following mordants?
(a) Al
3+
(b) Fe
3+
(c) Ba
2+
(d) Cr
3+
Assertion and Reason :
Each of the questions givenbelowconsists
of two statements, an assertion (A) and
Q.58
reason (R). Select the number R. Glucose and fruct ose
monosaccharides.
bot h are
corresponding to the appropriate
alternative as follows
Match the following
Q.59 Match list I with list II andselect the correct answer using the codes givenbelowthe lists.
List I
Nucleic acids
Uracil
Thymine
double-helix structure
A-(iv), B-(iii), C-(i), D-(i)
A-(iii), B-(i), C-(iv), D-(i)
List I
Pepsin
Nucleic acid
Ascorbic acid
Testosterone
List II
(i)
(ii)
(iii)
(iv)
(b)
(d)
A.
B.
C.
D.
(a)
(c)
D.N.A.
Hormones
Polynucleotides
R.N.A.
A-(iii), B-(iv), C-(i), D-(i)
none of these
List II Q.60
A.
B.
C.
D.
(i)
(ii)
(iii)
(iv)
(v)
Genetic material
Sexhormone
Vitamin C
Antibiotic
Digestive enzyme
(a)
(c)
A-(iv), B-(i), C-(iii), D-(ii)
A-(v), B-(i), C-(iii), D-(ii)
(b)
(d)
A-(v), B-(i), C-(ii), D-(iii)
none of these
25
Biomolecules
EXERCISE - III
Q.1
Q.8
Q.15
Q.22
Q.29
Q.36
Q.43
Q.50
Q.57
d
c
d
c
d
a
c
a
a
Q.2
Q.9
Q.16
Q.23
Q.30
Q.37
Q.44
Q.51
Q.58
d
a
c
a
b
a
d
b
b
Q.3
Q.10
Q.17
Q.24
Q.31
Q.38
Q.45
Q.52
Q.59
c
c
a
d
a
b
d
d
b
Q.4
Q.11
Q.18
Q.25
Q.32
Q.39
Q.46
Q.53
Q.60
c
d
c
a
d
c
c
b
c
Q.5
Q.12
Q.19
Q.26
Q.33
Q.40
Q.47
Q.54
a
d
d
a
(b,c,d)
a
c
a
Q.6
Q.13
Q.20
Q.27
Q.34
Q.41
Q.48
Q.55
b
c
c
b
c
b
d
c
Q.7
Q.14
Q.21
Q.28
Q.35
Q.42
Q.49
Q.56
b,c
b
a
b
b
a
c
c
ANSWERKEY
26