Bio – molecules

Carbohydrates: Optically active organic compounds which are polyhydroxy aldehydes or ketones or
the compounds which on hydrolysis gives these compounds. They have general formula C x(H2O)y, where
‘x and y can be 3,4,5 ---- etc. They occur naturally in animal and plant kingdom and are composed of
carbon, hydrogen and oxygen only.

Classification: Based on the taste, they are classified into two types

1. Sugars: These are the carbohydrates which are sweet in taste, water soluble and having
crystalline structure. Example: glucose, fructose, sucrose, maltose, lactose etc.
2. Non – Sugars: These are the carbohydrates which are tasteless, water insoluble and having
amorphous structure. Example: starch, cellulose, glycogen etc.

Classification of Sugar: The sugars are broadly classified into two types

1. Based on reducing property 2. Based on hydrolysed product

Based on reducing property:

1. Reducing sugars: sugars which will reduce Tollen’s and Fehling’s solution. Example:
glucose, fructose, maltose, lactose. This is because; they have free aldehyde or ketonic
group.
2. Non Reducing sugars: sugars which will not reduce Tollen’s and Fehling’s solution.
Example: Sucrose. This is because; they will not have free aldehyde or ketonic group.

Based on hydrolysed product:

1. Monosaccharides: These are the carbohydrates that cannot undergo hydrolysis. Example:
glucose, fructose, galactose, ribose etc.
These are classified into two types (1) based on functional group and (2) number of carbon
atoms.

Based on functional group:

a. Aldose: These are the monosaccharides which are having aldehyde group. Example:
glucose.
b. Ketose: These are the monosaccharides which are having ketonic group. Example:
factorise

Based on number of carbon atoms:

a. Triose: These are the monosaccharides which contains only three carbon atoms.
b. Tetrose: These are the monosaccharides which contains only four carbon atoms.
c. Pentose: These are the monosaccharides which contains only five carbon atoms.
d. Hexose: These are the monosaccharides which contains only six carbon atoms.
f. Heptose: These are the monosaccharides which contains only seven carbon atoms.

Note: Glucose is the example for aldohexose where as Fructose is the example for ketohexose.

2. Oligosaccharides: These are the carbohydrates which will give 2 – 9 units of

monosaccharides units on hydrolysis. Example: Sucrose, Maltose, Lactose.
a. Disaccharide: These are carbohydrates which will give two units of monosaccharides
on hydrolysis. Example: Sucrose, Maltose, Lactose
b. Trisaccharide: These are carbohydrates which will give three units of
monosaccharides on hydrolysis. Example: Rafinose (glucose + fructose + galactose)
3. Polysaccharides: These are carbohydrates which will give more than 9 units of
monosaccharides on hydrolysis. Example: starch, cellulose, glycogen.
Glucose:

Molecular formula: C6H12O6, Molecular mass: 180, It is a monomer of many large carbohydrates i.e.,
sucrose, lactose, maltose, starch, cellulose etc. It is also called as dextrose and present in sweet fruits,
honey. The ripe grape mainly contains glucose.

Preparation:

1. From sucrose (cane sugar): (Laboratory method) When sucrose is subjected to hydrolysis
by boiling it with dil. HCl/H2SO4 in alcoholic medium, glucose and fructose are obtained in
equal quantities.

C12H22O11 + H2O/H+ → C6H12O6 + C6H12O6

2. From starch: (Commercial method) When starch is subjected to hydrolysis by boiling it

with dil. H2SO4 under the pressure of 2 – 3 atmospheres at 393K, glucose obtains.

(C6H10O5)n + nH2O/H+ → nC6H12O6

Structure of glucose:

Molecular formula of glucose is C6H12O6

HI/ confirms six carbon atoms
CH 3 CH 2 CH 2 CH 2 CH 2 CH 3
are linked in a straight chain
n - Hexane
NH2OH
CH2OH(CHOH)4CH=NOH
Glucose oxime
confirms the presence of a
HCN CN carbonyl group
CH2OH(CHOH)4 CH
CHO Glucose cyanohydrin OH
Br2 /H2O
(CHOH)4 CH2OH(CHOH)4 COOH confirms the presence of a
Mild oxidation Gluconic acid aldehydic group
CH2OH
5(CH3CO)2O
Glucose OHC (CHOCOCH3)4 CH2OCOCH3 confirms the presence of a
Acetylation five - OH groups
Glucose pentaacetate
HNO3 confirms the presence of a
HOOC (CHOH)4COOH
Oxidation one primary alcoholic (- OH) group
Glucaric acid
(saccharic acid)

Open chain structure of glucose:

The open chain structure of glucose is given by Fischer. The glucose is generally
called as D (+) glucose. This is because with reference to the structure of
glyceraldehde, i.e., all those compounds which can be chemically related to (+)
isomer of glyceraldehyde are said to be ‘D’ and all those compounds which can
be chemically related to (-) isomer of glyceraldehyde are said to be ‘L’.

(+) indicates dextrorotatory nature provided – OH group of C5 atom is right side.

( - ) indicates laevorotatory nature provided – OH group of C5 atom is left side.

Cyclic structure of glucose: The open chain structure of glucose explains most of the properties but
not the following i.e.,

1. It will not give the positive test towards Schiff’s

test and also NaHSO3.
2. The pentaacetate of glucose does not reacts
with NH2OH to form oxime indicates absence
of – CHO group.
3. Existing of two forms of glucose i.e.,  and β is
not explained by open chain structure.

The above observations are due to existing of

hemiacetal structure of glucose which is six
membered ring in which – OH at C5 is involved in
ring formation with C1 carbon atom. Therefore the
two cyclic structure of glucose are known as Haworth structure

The two cyclic hemiacetal forms of glucose differ only in the configuration of the hydroxyl group at
C1 are called anomers of glucose, which are  - isomer (– OH group of C1 is towards right side) and β
– isomers (– OH group of C1 is towards left side).

Fructose: It is the ketohexose with molecular formula

C6H12O6. The ketonic group is present at C2 carbon
atom. It belongs to D – series and is a laevorotatory
compound. The Haworth structure of fructose is
known as furanose structure where the – OH go C5
carbon atom is added to C2 carbon atom.

Disaccharides:

Sucrose:

1. On hydrolysis gives equimolar mixture of  - D (+) –

glucosepyranose and β – D – (–) – fructofuranose.
2. Glycosidic linkage between C1 of glucose and C2 of
fructose
3. It is a non – reducing sugar because absence of free
carbonyl group.

Invert sugar: The hydrolysised product of sucrose which brings about a change in the sign of
rotation from dextro to laevo. This is because on hydrolysis sucrose give the mixture of
dextrorotatory glucose of + 52.50 rotation and laevorotation of fructose of – 92.40.

Maltose:

1. On hydrolysis give two units of  - D (+) –

glucosepyranose.
2. Glycosidic linkage is in between C1 of one glucose to
C4 of another glucose unit.
3. It is the reducing sugar because of presence of free
carbonyl group.
Lactose:

1. Known as milk sugar

2. On hydrolysis give one unit of β – D – galactose and one unit
of β - D – glucose.
3. The glycosidic linkage is between C1 of galactose with C4 of
glucose which is β – in nature.
4. It is a reducing sugar because of presence of free carbonyl
group.

NOTE: The linkage between two monosaccharide units through oxygen atom is called as glycosidic
linkage.

Polysaccharides: These are the carbohydrates which on hydrolysis gives more than nine
monosaccharides units. Example: starch, cellulose, glycogen etc.

1. Starch: Polymer of  - D – glucose units and consists of

two components amylase and amylopectin.
a. Amylase is water soluble, long unbranched chain of
 - D – (+) – glucose units held by 1,4 -  -
glycosidic linkage. It is present 20% of mass of
starch.
b. Amylopectin is water insoluble, branched chain
polymer of  - D – glucose units held by 1,4 -  -
glycosidic linkage whereas branching occurs by 1,6
-  - glycosidic linkage. It is present 80% of mass of
starch.
2. Cellulose:
a. It is most abundant organic substance in plant kingdom.
b. It is a predominant constituent of cell wall of plant cells.
c. Straight chain polysaccharide of β – D – glucose units joined together by 1,4 – β –
glycosidic linkage.

3. Glycogen:
a. It is also called as animal starch because its structure is similar to amylopectin but
highly branched one.
b. It is present in liver, muscles and brain of animals and also in yeast and fungi.
c. It will be broken down into glucose by enzymes when body needed the glucose.

Importance of carbohydrates:

1. Honey is used as instant source of energy in ayurvedic system of medicine.

2. It is used as storage molecules i.e., starch in plants and glycogen.
3. Cell wall of bacteria and plants i.e., cellulose used to build furniture, clothing in textile
industries, paper, lacquers and breweries.
4. These are present in DNA and some bio system in combination with many proteins and lipids.
Proteins:
Definition: These are the condensation polymers of  - amino acids which are essential for the growth
and maintenance of life.

General structural formula of  - amino acid:

Classification of amino acids:

Amino acids are broadly classified into three types i.e.,

1. Based on relative number of amino and carboxylic group in the molecules

a. Neutral amino acids: No. of – COOH groups = No. of – NH2 groups. Example: glycine,
alanine, valine
b. Acidic amino acids: No. of – COOH groups > No. of – NH2 groups. Example; aspartic
acid, asparagines, glutamic acid
c. Basic amino acids: No. of – COOH groups < No. of – NH2 groups. Example: lysine,
arginine, histidine etc.
2. Based on their synthesis in the body i.e., requirement.
a. Essential amino acids: Cannot be synthesised in the body and must be obtained
through diet. Example: valine, leucine, lysine, isoleucine, arginine, phenylalanine,
methionine, tryptophane, threonine and histidine.
b. Non – essential amino acids: Can be synthesised in the body. Example: glycine,
alanine, glutamic acid, aspartic acid etc.

Properties of amino acids:

1. They are colourless, crystalline solids soluble in water with high melting points and behave as
salts rather than amines or carboxylic acids.
2. Except glycine, all naturally occurring  - amino acids are optically active
because of presence of asymmetric  - carbon atom. Most of them naturally
occurs as L – configuration.
3. Zwitter ion: In aqueous solution, the carboxylic group can lose a proton and
amino group can accept a proton giving rise to a dipolar ion.
4. Peptide bond: It is the amide bond i.e., – CONH – formed between two amino
acids by the elimination of water molecule.
a. Dipeptide: Two amino acids are involved in formation of peptide bond with one peptide
bond.
b. Tripeptide: Three amino acids are involved in formation of peptide bond with two peptide
bonds.
c. Tetrapeptide: Four amino acids are involved in formation of peptide bond with three
peptide bonds.
d. Pentapeptide: Five amino acids are involved in formation of peptide bond with four
peptide bonds.
e. Hexapeptide: Six amino acids are involved in formation of peptide bond with five peptide
bonds.
f. Poly peptide: More than ten amino acids are involved in formation of peptide bond.

Example for dipeptide bond

O H O O H3C O
H2N CH2 C OH + H2N C C OH H2N CH2 C NH CH C OH
CH3
Glycine Glycinealanine
Alanine (Gly - Ala)
1. Amino acid containing primary alcoholic group : Serine
2. Amino acid containing secondary alcoholic group : Threonine
3. Amino acid containing thyol group (SH – group) : Cysteine
4. Amino acid containing thio group : Methionine
5. Amino acid containing phenolic group : Tyrosine
6. Amino acid containing phenyl group : Phenyl alanine
7. Amino acid/s containing amide group : Glutamine, Asparagine
8. Amino acid containing indole structure : Tryptophan
9. Amino acid/s containing heterocyclic structure : Tryptophan, Histidine, Proline
10. Amino acid/s containing five membered heterocyclic structures : Proline, Histidine
11. Amino acid containing one hetero atom : Proline
12. Amino acid containing imidazole structure : Histidine
Proteins: These are also called as polypeptide with more than hundred amino acids residues, having
molecular mass higher than 10,000 u.

Classification of proteins:

1. Fibrous proteins: In fibrous proteins, polypeptide chains run parallel and held together by
hydrogen and disulphide bonds. Example: keratin, myosin.
a. Keratin is present in hair, wool, nail
b. Myosin is present in muscles.
2. Globular proteins: in globular proteins, polypeptide chains coil around to give three
dimensional spherical shapes. These are soluble in water. Example: Insulin and albumins.

Structure of proteins: Structure and shape of proteins can be studied at four different levels

1. Primary structure: It refers to the specific sequence of  - amino acids held together in a
protein. Any change in this primary structure i.e., the sequence of amino acids creates a
different protein.
2. Secondary structure: Structures arise due to the regular folding of the backbone of the
polypeptide chain due to hydrogen bonding between – CO – and –NH2– groups of the peptide
bond. These are two types
a.  - Helix: Coils are stabilized by hydrogen bonds between carbonyl oxygen of first amino
acid to amide nitrogen of fourth amino acid.
b. β – Pleated sheet structure: intermolecular hydrogen bonds are formed between the
carbonyl oxygen and amide hydrogen of two or more adjacent polypeptide chains, giving
a β – pleated sheets structure. Example: silk fibroin.
3. Tertiary structure: This structure refers to overall folding of the polypeptide chains or its
complete 3D structure. This will give rise to two major molecular shapes which are stabilizes by
hydrogen bonds, disulphide linkage, van der Waals and electrostatic forces of attraction.
4. Quaternary structure: This structure refers to spatial arrangement of two or more polypeptide
chains with respect to each other.

Denaturation of proteins: When a protein in its native form is subjected to physical changes like
heating or chemical changes like changing pH of the solution, the hydrogen bonds are disturbed. Due to
this globules unfold and helix gets uncoiled and protein loses its biological activity.

The denaturation causes change in secondary and tertiary structure by primary structure
remains intact. Example: coagulation of egg white on boiling, curding of milk, formation of cheese etc.

Enzymes: These are the biocatalysts produced by living cells which catalyse the biochemical reactions
in living organisms.
Enzymes Reaction catalysed
Properties of enzymes: Maltase Maltose → glucose + glucose
Lactase Lactose → glucose + galactose
1. Required in very small amount. Amylase Starch → n x glucose
2. They reduce magnitude of activation Invertase Sucrose → glucose + fructose
energy.
Pepsin Proteins →  - amino acids
3. They are highly specific
Trypsin Proteins →  - amino acids
4. They work at specific pH.
Urease Urea → CO2 + NH3
5. They work well at moderate
Nuclease DNA, RNA → nucleotides
temperature.
6. Action of Enzyme: (Mechanism)
Binding of the enzyme (E) to substrate (S) to form a complex called the enzyme – substrate
complex.
E + S → ES
Formation of complex of enzyme and product ES → EP
Release of product from the enzyme – product complex EP → E + P
 Hormones: These are the intercellular messengers which are produced by endocrine glands in the
body and are poured directly in the blood stream which transports them to the site of action.

Classification of hormones:

1. Hormones of steroids type: Estrogens and Androgens

2. Hormones of poly peptide type: Insulin and Endorphins
3. Hormones of amino acids derivative type: Epinephrine and Norepinephrine.

The main role of hormones in the body is to maintain the balance of biological activities in the body.
Role of some important hormones are as follows

1. Insulin: It contains 51 amino acids and produced by β – cells of pancreas which regulates the
glucose level in the blood along with glucagon hormone.
2. Epinephrine and Norepinephrine: These two hormones will mediate responses to external
stimulation.
3. Growth and Sex hormones: These two hormones will helps in the growth and development of
the organism.
4. Thyroxin: This hormone will regulate the iodine level in the body and it is produced by thyroid
glands.
a. Hypothyroidism: It is caused due to low production of thyroxin in the body which leads
to lethargyness and obesity for the organism.
b. Hyperthyroidism: It is caused due to high production of thyroxin in the body and taking
low quantity of iodine through diet which leads to enlargement of thyroid gland. This
disease is controlled by taking commercial table salt i.e., iodised salt.
5. Steroid hormones: These hormones are produced by adrenal cortex and gonads (testes in males
and ovaries in females)
a. Hormones released by adrenal cortex: These hormones help us in the functions of
body.
i. Glucocorticoids: This hormone controls the carbohydrate metabolism, modulates
inflammatory reactions and involved in reactions of stress.
ii. Mineralocorticoids: This hormone controls the excretion of water and salt by the
kidney.

Improper function of adrenal cortex: This causes a disease known as Addison’s due to
which the person gets hypoglycaemia, weakness and increased susceptibility to stress.

Remedy: By giving the proper dosage of glucocorticoids and mineralocorticoids.

b. Hormones released by gonads: These hormones are responsible for development of

secondary sex characters of organisms.
i. Testosterone: The secondary sex hormones produced by males which helps in
development of secondary male characteristics in the child i.e., deep voice, facial
hair, general physical constitution.
ii. Estradiol: The main sex hormone produced by female which are responsible for
development of secondary female characteristics and participates in the control of
menstrual cycle.
iii. Progesterone: This hormone is responsible for preparing the uterus for
implantation of fertilised egg.
Vitamins: The organic compounds taken trough the diet in small quantities to perform specific
biological functions for normal maintenance of optimum growth and health of the organism.

Classification of vitamins: These are classified into two types

1. Water soluble vitamins: vitamin – B and vitamin – C. these two vitamins are regularly taken
through food because they are not stored in body and excreted from the body through urine.
2. Fat soluble vitamins: Vitamin – A, Vitamin – D, Vitamin – E, and Vitamin – K. These
vitamins are stored in liver and adipose tissues.

Some important vitamins, their sources and their deficiency diseases:

Vitamin name Chemical name Sources Deficiency disease

Milk, butter, eggs, fish,
Night – blindness, xerophthalmia
Vitamin – A Retinol cod liver oil, green
(hardening of cornea of eye)
vegetables etc
Pulses, nuts, cereals,
Beri – beri, loss of appetite, retarded
Vitamin – B1 Thiamine yeast, egg yolk, green
growth
vegetables
Anaemia, inflammation of tongue,
Milk, green vegetables,
dermatitis, cheilosis (fissuring at corners
Vitamin – B2 Riboflavin egg white, meat, liver,
of mouth and lips) digestive disorders
kidney etc
and burning sensation of the skin.
rice bran, whole cereal, Affects central nervous system,
Vitamin – B6 Pyridoxine
yeast, fish, meat, eggs etc weakness, convulsions
Eggs, milk, liver of ox, Pernicious anaemia (RBC deficient in
Vitamin – B12 Cyanocobalamin
sheep, fish haemoglobin)
Citrus fruits, chillies,
Vitamin – C Ascorbic acid Pyorrhoea, scurvy (bleeding of gums)
sprouted pulses,
Ergocalciferol
Butter, milk, eggs, fish Rickets (bending of bones) and
Vitamin – D and
liver oil, liver and meat osteomalacia
cholecalciferol
Wheat germ oil, milk,
Loss of fertility in males, muscles
Vitamin – E Tocopherol nuts, peanut oil, cotton
degeneration
seed oil, eggs, fish
Leafy vegetables like Haemorrhages and lengthens time of
Vitamin – K Phylloquinone
cabbage, spinach blood clotting.

NOTE: Vitamin – H or vitamin – B7 (Biotin) it is water soluble, present in milk, yeast, liver, kidney,
deficiency causes dermatitis disease.

Nucleic Acids: These are the polymers of nucleotides present in nucleus of all living cells and play an
important role in transmission of the hereditary characteristics and biosynthesis of proteins.

Classification:

Nucleic Acid
Messenger RNA
[m - RNA]

Deoxyribonucleic Acid Ribonucleic Acid Ribosomal RNA

[DNA] [RNA] [r - RNA]

Transfer RNA
[t - RNA]
Structure of Nucleic acid:
Nucleoside
1. Nucleoside: A unit formed by attachment of a base to 1’ position of sugar. 5'
Base
OH - CH2
O
H 4' H 1'
2. Nucleotide: When nucleoside is linked to phosphoric acid at 5’ position of sugar
H H
moiety. One unit of nucleotide is having pentose sugar, nitrogenous base 3' 2'
O
and phosphate group, i.e., Nucleotide
OH OH
5'
-
O - P - O - CH2 Base
Nucleotide → Pentose sugar + Nitrogenous base + Phosphate group O
Nucleotides are joined together by phosphodiester linkage between 5’ O- 4' H H 1'
and 3’ carbon atoms of pentose sugar. H H
3' 2'

Nitrogenous Base OH OH

Pyrimidine Purine

Thymine Cytosine Adenine Guanine

Uracil (U) (G)
(T ) (C) (A)
O O NH2 NH2 O
H3C N N
NH NH N N NH

NH O NH O NH O NH N NH N NH2

Primary structure: Refers to the sequence of nucleotides in the chain of nucleic acid.

Secondary structure: Two strands of polynucleotides coil around each other in the form of double
helix. James Watson and Francis Crick gave a double strand helix structure for DNA.

Difference between DNA and RNA

Components DNA RNA

Sugar 2 – deoxy – D – ( - ) ribose D – ( - ) ribose
Pyrimidine base Cytosine and thymine Uracil and cytosine
Structure Double stranded  - helix Single stranded  - helix
Replication Possible Not possible
Bases Adenine, guanine, cytosine, thymine Adenine, guanine, cytosine, uracil
Biological functions:

1. Replication: Single DNA molecule produces two identical copies of itself.

2. Protein synthesis: It is carried out by RNA molecules in two steps
a. Transcription: Synthesis of RNA from DNA in the cytoplasm
b. Translation: Protein synthesis by RNA molecules.

DNA Fingerprinting:

1. Every individual has unique fingerprints.

2. The unique fingerprints are due to unique sequences of bases on DNA for every person.
3. The technique for identifying individual person based upon the uniqueness of their DNA pattern
is called DNA fingerprinting.