Biomolecules

MOHMMED.ILIAS

1. Carbohydrates: Major energy source, storage molecules like starch in plants.

These are optically active polyhydroxy aldehydes or ketones or the compounds which produce
these on hydrolysis.
2. Classification based on hydrolysis
a. Monosaccharides : Those carbohydrates which cannot be hydrolysed into further
simpler carbohydrates. E.g., glucose, fructose, galactose, etc.
b. Disaccharides: Those carbohydrates which produce two monosaccharides on hydrolysis.
E.g., sucrose, maltose and lactose.
c. Oligosaccharides: Those carbohydrates which give two to ten monosaccharides on
hydrolysis.
d. Polysaccharides: Those carbohydrates which on hydrolysis give the large number of
monosaccharides hydrolysis. E.g., starch, cellulose, glycogen.
3. Sugar: Carbohydrates which are sweet in taste.
a. Reducing sugars: Those which reduce Fehling’s or Tollen’s reagent due to availability of
free aldehydic groups. E.g., glucose, fructose, galactose.
b. Non-reducing sugars: Those which do not reduce Fehling’s or Tollen’s reagent. They do
not have free aldehydic group. E.g., sucrose.
4. Glucose: It is a monosaccharide with molecular formula C6 H12O6
5. Preparation

6. Structure
Fischer structure : (+) glucose has ‘D’ configuration as shown :

‘D’- means – OH group on first chiral ‘C’ from the bottom is on the
right hand which is relative to d -glyceraldehyde and (+) means it
is dextrorotatory i.e., it rotates plane-polarized light towards right

7. Reactions of glucose:
reaction inference
GLUCOSE E + HI Hexane Glucose contains six carbon atoms
GLUCOSE E + HCN Glucose cyanohydrin Glucose contains carbonyl group
GLUCOSE + NH2OH Glucose Oxime
 Glucose + Bromine
Glucose + con HNO3
Glucose + Acetic anhydride
glucose
Gluconic acid Glucose contains an aldehydic
group
Saccharic acid Glucose contains an aldehydic
group and primary alcohol
Penta acetate of Glucose contains five OH groups

8. Objections against the open chain structure of glucose

The open chain structure was unable to explain the following reactions :
a) It does not give the 2, 4-DNP test, Schiff’s test and does not form the hydrogensulphite
product with NaHSO3
b) The pentacetate of glucose does not react with NH2OH, indicating the absence of free
aldehydic group.
c) Glucose exist in 2 different crystalline forms α and β forms. These are called anomers. They
differ in optical rotation, they also differ in melting point.

After which a close chain (cyclic) structure of glucose was proposed by Haworth.
αD –(+) Glucopyranose βD –(+) Glucopyranose
* Anomers are isomers which have a different configuration at C-1 functional
group c-atom

Fructose

Fructose occurs in fruits and it is called the fruit sugar.

• C6H12O6
• It contains the keto group at C-2
• Leave rotatory

Haworth projection of fructose

 D –(-)Fructofuranose Β D –(-) Fructofuranose

* Epimers are isomers which have a different configuration at C-2 functional

group c-atom
 Disaccharides

Glycosidic linkage:

glycosidic linkage: The oxide linkage formed by the loss of a water molecule when two
monosaccharides are joined together through oxygen atom is called a glycosidic linkage

Lactose

• It is composed of β-D-galactose (left) and β-D-glucose (right).

• There is a β-glycosidic linkage between the C1 of galactose and C4 of glucose unit. It
is a reducing sugar.

• Sucrose
• It is composed of α-D-glucose and β-D-fructose
• glycosidic linkage between the C1 of Glucose and C2 of Fructose unit.
• It is a non-reducing sugar.
Sucrose is a non-reducing sugar as the reducing groups (carbonyl groups) of glucose
and fructose are involved in glycosidic bond formation
•
• Why is sucrose called invert sugar?
Ans. When sucrose is hydrolysed by water, the optical rotation of solution changes
from positive to negative

Maltose

• It is a disaccharide made up of two alpha D glucose

• the bond that joins two alpha glucose units is called alpha 1,4 glycosidic linkage.
• At C1 of the second glucose unit, an aldehyde group can be formed in solution,
which makes maltose a reducing sugar.

POLYSACCHARIDES
• Cellulose is the most abundant organic compound on earth with a chemical
formula (C6H10O5)n.
• Cellulose mainly αcurs in plants. The cell wall of plant cells is made up of cellulose.
It is a long-chain polymer.
• In cellulose, β-D-glucose units are linked by glycosidic linkage between C1 -of one
unit of glucose and C4 of another glucose unit.
• Water insoluble
• Starch: It is a polymer of -glucose and consists of two components — Amylose and
Amylopectin.
• Amylose:
1. It is a water-soluble component
2. It is a long unbranched chain polymer
3. It contains 200 – 1000 -D-(+)- glucose units held by – glycosidic linkages involving C1 –
C4glycosidic linkage
4. It constitutes about 15-20% of starch
• Amylopectin
1. It is a water insoluble component
2. It is branched chain polymer
3. It forms chain by C1 – C4glycosidic linkage whereas branching occurs by C1 – C6glycosidic
linkage
4. It constitutes about 80-85% of starch
• Glycogen:
1. The carbohydrates are stored in animal body as glycogen.
2. It is also known as animal starch because its structure is similar to Amylopectin.
3. It is present in liver, muscles and brain.
4. When the body needs glucose, enzymes break the glycogen down to glucose.
Protein:
Polypeptide chain where many amino acids are joined together by a peptide bond
Amino acids:
• Amino acids contain amino (–NH2) and carboxyl (–COOH) functional groups.
• All are optically active except glycine

Where R – Any side chain

Most naturally occurring amino acids have L – Config.
• Types of amino acids:
a). Essential amino acids: The amino acids which cannot be synthesised in the body and must
be obtained through diet, are known as essential amino acids. Examples: Valine,
Leucine
b). Non-essential amino acids: The amino acids, which can be synthesised in the body, are
known as non-essential amino acids. Examples: Glycine, Alanine

• Zwitterion form of amino acids:

1. Amino acids behave like salts rather than simple amines or carboxylic acids. This behaviour
is due to the presence of both acidic (carboxyl group) and basic (amino group) groups in
the same molecule. In an aqueous solution, the carboxyl group can lose a proton and
amino group can accept a proton, giving rise to a dipolar ion known as zwitter ion. This is
neutral but contains both positive and negative charges.
2. In zwitterionic form, amino acids show amphoteric behaviour as they react both with acids
and bases.
3. In zwitterionic form Due to this dipolar behavior they have strong electrostatic
interactions within them. For this reason melting point of amino acids is high

• Isoelectronic point: The pH at which the dipolar ion exists as neutral ion and does not
migrate to either electrode cathode or anode is called isoelectronic point.
• Proteins: Proteins are the polymers of -amino acids and they are connected to each
other by peptide bond or peptide linkage. A polypeptide with more than hundred amino
acid residues, having molecular mass higher than 10,000u is called a protein.
• Peptide linkage: Peptide linkage is an amide linkage formed by condensation reaction
between –COOH group of one amino acid and –NH2 group of another amino acid.

•
• Primary structure of proteins: The sequence of amino acids is said to be the primary
structure of a protein.
• Secondary structure of proteins: It refers to the shape in which long polypeptide chain can
exist. Two different types of structures:
– Helix

∞ Right-handed screw with the NH group of each amino acid residue intra molecular H
– bonded to – C = O of adjacent turn of the helix.

– pleated sheet
In this conformation, all peptide chains are stretched out to nearly maximum extension
and then laid side by side which are held together by intermolecular hydrogen bonds.
• Tertiary structure of proteins: It represents the overall folding of the polypeptide chain
i.e., further folding of the 2° structure.
• Types of bonding which stabilize the 3° structure:
1. Disulphide bridge (-S – S-)
2. H – bonding – (C = O … H – N)
3. Salt bridge (COO– … + )
4. Hydrophobic interactions
5. van der Waals forces

Tw shapes of proteins:
Fibrous proteins
a) When the polypeptide chains run parallel and are held together by hydrogen and
disulphide bonds, then fibre– like structure is formed.
b) These proteins are generally insoluble in water
c) Examples: keratin (present in hair, wool, silk) and myosin (present in muscles), etc

Globular proteins
a) This structure results when the chains of polypeptides coil around to give a spherical
shape.
b) These are usually soluble in water.
c) Examples: Insulin and albumins

• Quaternary structure of proteins:

1. Some of the proteins are composedof two or more polypeptide chains referred to as sub-
units.
2. The spatial arrangement of these subunits with respect to each other is known as
quaternary structure of proteins.
• Proteins found in a biological system with unique 3D-structure and biological activity is
called native protein.
• Denaturation of proteins:
1. The loss of biological activity of proteins when a protein in its native form, is subjected to
physical change like a change in temperature or chemical change like change in pH. This is
called denaturation of protein.
2. Example: coagulation of egg white on boiling, curdling of milk.
 • Nucleoside:
1. Nitrogenous Base + pentose sugar

• Nucleotide:
1. Nitrogenous Base + pentose sugar + phosphate group

• two types of nucleic acids:

• DNA
1. It has a double-stranded -helix structure in which two strands are coiled spirally in
opposite directions.
2. Sugar present is –D–2-deoxyribose
3. Bases:
i) Purine bases: Adenine (A) and Guanine (G)
ii) Pyrimidine bases: Thymine (T) and cytosine (C)
4. It occurs mainly in the nucleus of the cell.
5. It is responsible for transmission for heredity character

RNA
1. It has a single stranded -helix structure.
2. Sugar present is –D–ribose
3. Bases:
i) Purine bases: Adenine (A) and Guanine (G)
ii) Pyrimidine bases: Uracil (U) and cytosine (C)
4. It occurs mainly in the cytoplasm of the cell.
5. It helps in protein synthesis.
6. Three main types of RNA are involved in protein synthesis. They are messenger RNA
(mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). rRNA forms ribosomes, which
are essential in protein synthesis.

Double helix structure of DNA:

a) It is composed of two right handed helical polynucleotide chains coiled spirally in opposite
directions around the same central axis.
b) Two strands are held together by H – bonds (A = T, G C).
c) The two strands are complementary to each other because the hydrogen bonds are formed
between specific pairs of bases.
d) Adenine forms hydrogen bonds with thymine whereas cytosine forms hydrogen bonds with
guanine.
e) Diameter of double helix is 2 nm.
f) Double helix repeats at intervals of 3.4 nm. (One complete turn)
g) Total amount of purine (A + G) = Total amount of pyramidine (C + T)

• vitamins:
• Vitamins are organic compounds required in the diet in small amounts to perform specific
biological functions for normal maintenance of optimum growth and health of the
organism.
• Classification of vitamins: Vitamins are classified into two groups depending upon their
solubility in water or fat.
1. Water soluble vitamins i) These vitamins are soluble in water.
ii) Water soluble vitamins must be supplied regularly in diet because they are readily
excreted in urine and cannot be stored (except vitamin B12) in our body.
iii) Example: Vitamin C, B group vitamins.
2. Fat soluble vitamins
i) These vitamins are soluble in fat and oils but insoluble in water.
ii) They are stored in liver and adipose (fat storing) tissues.
iii) Example: Vitamin A, D, E and K

Important vitamins, their sources and their deficiency diseases:

Name of
Sources Deficiency diseases
vitamins

xerophthalmia
Fish liver oil, carrots, butter
Vitamin A (hardening of cornea of eye)
and milk
Night blindness

Vitamin B1 Yeast, milk, green vegetables Beriberi

(Thiamine) and cereals (loss of appetite, retarded growth)

Cheilosis
Vitamin B2
Milk, egg white, liver, kidney (fissuring at corners of mouth and lips), digestive
(Riboflavin)
disorders and burning sensation of the skin.

Vitamin B6 Yeast, milk, egg yolk, cereals

Convulsions
(Pyridoxine) and grams
 Pernicious anaemia
Vitamin B12 Meat, fish, egg and curd
(RBC deficient in haemoglobin)

Vitamin C Citrus fruits, amla and green Scurvy

(Ascorbic acid) leafy vegetables (bleeding gums)

Rickets
Exposure to sunlight, fish and (bone deformities in children) and
Vitamin D
egg yolk osteomalacia
(soft bones and joint pain in adults)

Vegetable oils like wheat germ

Vitamin E Increased fragility of RBCs and muscular weakness
oil, sunflower oil, etc.

Vitamin K Green leafy vegetables Increased blood clotting time

REVISION QUESTIONS

QUESTION BANK BIOMOLECULES

1. Define
a. Fibrous protein 2020 j. Anomers 2019
b. Invert sugar 2020, 2019, k. Essential amino acids 2019
2010(D) l. Tertiary structure of protein
c. Native protein 2020, 201 2019
d. Polysaccharides 2020, 2019 m. Disaccharides 2019
e. Glycosidic linkage 2020, n. Denatured protein 2019
2009(D) o. . Peptide Linkage
f. Oligosaccharides 2020, 2019 2019,2012,2009(D), 2008(D)
g. Denaturation of protein p. Primary structure 2014
2020, 2019, 2008(D) q. Biocatalyst 2014
h. Vitamins 2019 r. Polypeptides 2010(D)
i. Nucleotide 2019 s. Phosphodiesterase linkage
2. Give the significance of (+) sign in the name D-(+)-glucose.
3. Name the amino acid which is not optically active.
4. Where does the water present in the egg go after boiling the egg ?
5. Give one example of : (a) water soluble, (b) fat soluble vitamins
6. Mention two important functions of carbohydrates in plants
7. What are the products of hydrolysis of lactose/Maltose /Sucrose ?
8. The two strands in DNA are not identical but complementary. Explain
9. List the reactions of glucose which cannot be explained by its open chain structure
10. Name the constituents of starch and what is the difference between them ?
11. Why cannot vitamin C be stored in our body ?

12. Differentiate between the following

a. Amylose and Amylopectin 2020, 2019
b. Globular protein and Fibrous protein 2020, 2019, 2015
c. Nucleotide and Nucleoside 2020, 2019, 2016(D)
d. Peptide linkage and Glycosidic linkage 2020
e. Essential amino acids and Non-essential amino acids 2019
f. Starch and glucose 2019
g. DNA and RNA 2019
h. Native and denatured protein 2019
13. Give a plausible explanation for the following :
a. Glucose doesn’t give 2,4-DNP test.
b. The two strands in DNA are not identical but are complementary.
c. Starch and cellulose both contain glucose unit as monomer, yet they are
structurally different
d. . What are amino acids ?
e. Why are amino acids amphoteric?
f. Give one point of difference between acidic and basic amino acid.
g. Name the linkage formed when carboxyl end of one amino acid condenses with
the amino end of other amino acid
h. Name the disaccharide which on hydrolysis gives two molecules of glucose. 2020
i. Name the disaccharide which on hydrolysis gives glucose and galactose. 2020
j. Name the vitamin whose deficiency causes convulsions. 2020 8.
k. How can you explain the absence of an aldehyde group in the pentaacetate of D-
glucose ?
l. Name the bases present in RNA. Which one of these is not present in DNA
m. Write chemical reactions to show that open structure of D-glucose contains the
following : (i) Straight chain (ii) Five alcohol groups (iii) Aldehyde as carbonyl group
n. What type of bonding provides stability to -helix structure of protein
o. Which one of the following is a disaccharide : Glucose, Lactose, Amylose, Fructose
p. Write the name of the vitamin responsible for the coagulation of blood.
q. Write the main structure difference between DNA and RNA. Of the four bases,
name those which are common to both DNA and RNA
r. Vitamin ‘C’ is a vitamin found in fruits and vegetables. It cannot be stored in our
body. Why?
s. Draw the Haworth structure of maltose, lactose and sucrose
t. Glucose is D + glucose .what does D and + indicates?
u. How is glycogen different from starch?
v. What are different types of RNA which are found in the cell?
w. Name the following vitamins and diseases caused by these vitamins
i. Fat soluble
ii. Water soluble