Bio Molecules - Chemistry Class 12 (CBSE)
Bio Molecules - Chemistry Class 12 (CBSE)
Bio Molecules - Chemistry Class 12 (CBSE)
BIOMOLECULES
Biomolecules are the organic compounds which form the basis of
life, i.e., they build up the living system and responsible for their
growth and maintenance.
*Monosaccharide
*Oligosaccharide
*Polysaccharide
Monosaccharides:
✓ These are simplest carbohydrate which can’t be hydrolyzed further into smaller compounds.
✓ They are called as aldose or ketose depending upon whether they have aldehyde or ketone
group.
✓ Depending upon the number of carbon atoms present they are called as triose, tetrose etc.
Contd…
Oligosaccharides:
These carbohydrates on hydrolysis give 2 to 10 molecules of monosaccharides.
They are further of few types:
•Disaccharides (C12H22o11): On hydrolysis, they give 2 molecules of
monosaccharides which are held together by Glycosidic linkage. Example:
sucrose etc.
•Trisaccharides (C18H32o16): On hydrolysis, they form three molecules of
monosaccharides. Example: raffinose
•Tetra-saccharides: (C24H42o21): Such as stachyose which gives four
monosaccharides on hydrolysis.
Polysaccharides:
These are the carbohydrates which on hydrolysis, yield more than ten
monosaccharides molecules. Example: Starch, Cellulose, Glycogen etc.
Preparation of Glucose :
i) By hydrolysis of starch with hot dil mineral acids.
Contd..
• ii) Reaction with hydrogen cyanide (HCN):
*** ‘D’ and ‘L’ have no relation with the optical activity of the compound but
represents configuration.
D- and L- ???
•Glyceraldehyde (for reference) contains one asymmetric carbon atom
and exists in two enantiomeric forms.
(2) The pentaacetate of glucose doesn’t react with hydroxylamine. This indicates
that free -CHO group is absent from glucose molecule.
Glucose is found to exist in two different crystalline forms which are named as
α and β.
The α-form of glucose (m.p. 419 K) is obtained by crystallization from
concentrated solution of glucose at 303 K while the β-form (m.p. 423 K) is
obtained by crystallization from hot and saturated aqueous solution at 371 K.
Anomers :
In α-D-glucose, the OH group at C1 is towards right while in β-D-glucose, the OH
group at C1 is towards left. Such a pair of stereoisomers which differ in
configuration only around C1 are called anomers and the C1 carbon is
called Anomeric carbon (or glycosidic carbon).
Haworth Ring Structures of Glucose and Fructose -
Glucose Fructose
• ***In zwitter ionic form, amino acids show amphoteric behaviour as they
react both with acids and bases.
Peptides
Peptides are condensation products of two or more amino acids.
Peptide Linkage
Peptide linkage is an amide linkage formed by condensation of two amino acids
involving −NH2 group of one amino acid and the −COOH group of the other amino
acid with the loss of water.
Classification of Peptides:
• On the basis of number of amino acids undergoing the
condensation, the peptides can be classified as:
o Dipeptide: It is a peptide composed of two amino-
acid residues.
o Tripeptide: It is a peptide composed of three amino-
acid residues.
o Polypeptide: It is a peptide composed of more than
ten amino-acid residues.
Protein
Peptide having molecular mass higher than 10,000 u is called a protein.
(Insulin – 51 aminoacids)
Classification of Proteins
• On the basis their molecular shape, proteins can be classified as:
o Fibrous proteins: The polypeptide chains run parallel and are held
together by hydrogen and disulphide bond forming a fibre like structure.
They are generally insoluble in water.
For example: Keratin (present in hair, wool, silk) and myosin (present in
muscles), etc.
o Globular proteins: The polypeptide chains coil around to give a spherical
shape. These are soluble in water.
For example: Insulin and albumins.
Structure of Proteins
• Primary structure: The sequence of amino acids is said to be the primary
structure of a protein.
• Secondary structure: This structure of a protein refers to the shape in
which a long polypeptide chain can exist.
There are two secondary structures of proteins:
o α-Helix: In α-Helix, the polypeptide chain coil itself into a righthanded
screw with the −NH group attached to the −C=O of an adjacent turn of
the helix by the intramolecular hydrogen bonding.
It generally exists when R- group is large
o β-Helix: In this structures, the peptide chains are stretched out to
nearly maximum extension and then laid side by side, held together by
intermolecular hydrogen bonds.
It generally exists when R- group is small.
Contd…
• Tertiary structure: The tertiary structure of proteins represents overall
folding and superimposition of the polypeptide chains, i.e., further folding
of the secondary structure giving rise to a ball shape or spheroidal shape
structure.
It is stabilised by covalent, ionic, hydrogen and disulphide bonds.
• Quaternary structure: Some of the proteins are composed of two or
more polypeptide chains referred to as sub-units. The spatial arrangement
of these subunits with respect to each other is known as quaternary
structure.
Denaturation of Proteins***
• The most stable conformation of a protein at a given temperature and the pH
is known as its native state.
• The loss of biological activity of proteins when a protein in its native form, is
subjected to physical change like change in temperature or chemical change
like change in pH, is called denaturation of protein.