Professional Documents
Culture Documents
Biomolecules
Carbohydrates:
Most carbohydrates have the general formula Cx(H2O)y
Classification of carbohydrates: Three groups (on the basis of their behaviour on
hydrolysis)
Monosaccharides: Cannot be hydrolysed further to yield simpler units;
Example: glucose, fructose
Oligosaccharides: On hydrolysis, give two to ten units of
monosaccharides
Disaccharides (give two units)
Example: sucrose (gives glucose and fructose) maltose (gives two
molecules of glucose)
Trisaccharides (give three units)
Tetrasaccharides (give four units), etc.
Polysaccharides: On hydrolysis, give a large number of units of
monosaccharides
Called non-sugars as they are not sweet to taste
The carbohydrates which are sweet to taste are also called sugars.
Glucose:
Fructose:
Molecular formula, C6H12O6
Structure
Cyclic structure (Haworth structure)
Disaccharides:
Glycosidic linkage Linkage between two monosaccharide units through oxygen atom
Sucrose
Lactose
It is also know as milk sugar (as it is found in milk)
Polysaccharides:
Starch
Main storage polysaccharide of plants
Two components – Amylose and amylopectin
Cellulose
Predominant constituent of cell wall of plant cells
Glycogen
Storage carbohydrates of animals
Known as animal starch
Proteins:
Amino acids
One-
Name of the Characteristic feature Three-letter
letter
amino acids of side chain, R symbol
code
Glycine H Gly G
Alanine –CH3 Ala A
Valine* (H3C)2CH– Val V
Leucine* (H3C)2CH–CH2– Leu L
H 3C CH 2 CH
Isoleucine* | Ile I
CH 3
HN C NH CH 2 3
–
Arginine* | Arg R
NH 2
Lysine* H2 N CH 2 4
Lys K
Glutamic acid HOOC CH2 CH2 Glu E
Aspartic acid HOOC–CH2– Asp D
Glutamine Gln Q
Asparagine Asn N
Threonine* H3C–CHOH– Thr T
Serine HO–CH2– Ser S
Cysteine HS–CH2– Cys C
Methionine* H3C–S–CH2–CH2– Met M
Phenylalanine* C6H5– CH2– Phe F
Tyrosine (p)HO–C6H4–CH2– Tyr Y
Tryptophan* Trp W
Histidine* His H
Proline Pro P
Structure of proteins:
Peptide linkage Amide formed between –COOH group and –NH2
group
Insulin contains 51 amino acids.
Classification of proteins (based on their molecular shape)
Fibrous protein
Parallel polypeptide chains are held together by hydrogen and
disulphide bonds. Generally, they are insoluble in water.
Example: keratin, myosin
Globular protein
Coil of polypeptide chains of spherical shape. Generally, they are
soluble in water. Example: insulin, albumin
Primary structure of protein –
Sequence of amino acids in polypeptide chain
Secondary structure of protein –
Due to regular folding of polypeptide chain on account of
H-bonding
–helix
–pleated
Tertiary structure of protein –
Overall folding of the polypeptide chains
Quaternary structure of protein –
Spatial arrangement of subunits with respect to each
other
Denaturation of protein: Loss of biological activity by a protein as a result
of unfolding of globules and uncoiling of helix. Example: coagulation of egg on
boiling, curdling of milk
Enzymes: Biocatalysts
Maltase
C12 H 22 O11 2C6 H12 O6
Glucose
Oxidoreductase: Enzymes which simultaneously catalyse the
oxidation of one substrate and the reduction of another substrate
Enzymes reduce the magnitude of activation energy of a reaction
Vitamins:
Organic compounds required in small amounts in the diet, whose deficiency causes
specific diseases.
Classification of vitamins
Fat-soluble vitamins: Vitamins A, D, E and K
Water-soluble vitamins: Vitamin C and B group vitamins
Formation of dinucleotide
Primary structure –
Sequence of nucleotides in the chain
Secondary structure –
Double-strand helix structure for DNA: The two strands are
complimentary. This is because H–bonds are formed between
specific pairs of bases.
A–T
C–G