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BIOMOLECULES

PREPARED BY
S RATH PGT BIO
K V III BBSR

http://students-learn.blogspot.com/

BIOMOLECULES-CLASS XI BIOLOGY 1
Biomolecules of cells
 All carbon compounds that are found in
the living tissues are called Biomolecules.
 Example-carbohydrate, fat, protein, amino
acids, lipids etc.

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Classification of
Biomolecules
BIOMOLECULES

MICROMOLECULES MACROMOLECULES
Mol. Wt.< 1000 Mol. Wt. >1000

Amino acid nucleotides


Polysaccharides, proteins
Sugars , lipids
Nucleic acids
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Amino acids

 These are organic compounds which


contain an amino group and an acidic
group .
 They are substituted methane with 4
substituent groups occupying the 4
valency positions of the carbon; these
are hydrogen, carboxyl group, amino
group & a variable group designated as
R group.

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Amino acids

 There are 20 amino acids occur in protein.


 A specific characteristic property of amino
acids is the ionizable nature of amino and
carboxyl group, so the structure of amino
acids changes in solutions of different pHs.

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Types of amino acids
 Basic – lysine arginine
 Acidic – glutamic acid aspartic acid
 Neutral – alanine glycine valine
 Aromatic – phenyl alanine , tyrosine,
tryptophan

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Sugars

 Simplest sugars are monosaccharides,


which cannot be hydrolysed further
composed of 3-7 carbon atoms. E.g.
glyceraldehydes, ribose, glucose,
fructose etc.
 They have either free aldehyde or
ketone group which reduce cupric ion to
cuprous ion ,called reducing sugar.
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Sugars

 Oligosaccharides may have two or a few


monosaccharides.
 Bond between two monosaccharides is
called glycosidic bond.

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lipids
lipids

Straight chain Fused hydrocarbon


compound Ring e.g. cholesterol

simple compound

oil phospholipids

fats glycolipids

waxes
BIOMOLECULES-CLASS XI BIOLOGY
sphingolipids 9
Nucleotides
 Organic compounds with heterocyclic rings.
 A nucleotide consists of a nitrogenous base, a
pentose sugar and a phosphate group.
 A nucleoside has a nitrogenous base attached to
a pentose sugar.
 The nitrogenous bases are called adenine,
guanine, thymine, cytosine and uracil
 Polymerised nucleotides form DNA and RNA
which are the genetic material.

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Primary and secondary
metabolites
 Metabolites may be primary or secondary type.
 Primary metabolites have identifiable functions
and play specific roles in the normal physiological
processes. E.g. amino acids, nitrogenous bases,
nucleic acids etc.
 Secondary metabolites are products of certain
metabolic pathways. E.g. pigments, rubber, gums,
resins, carotenoids etc.

BIOMOLECULES-CLASS XI BIOLOGY 11
Polysaccharides
 These are a class of organic compounds
(carbohydrates) which are long chain polymers
of monosaccharides.
 They are of two types: homopolysaccharides,
heteropolysaccharides
 Homopolysaccharides- cellulose, starch, inulin
 Heteropolysaccharides- chitin

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Proteins
 They are heteropolymers containing a string or
strings of amino acids.
 A peptide bond formed between the carboxyl
group and the amino group of successive amino
acids, joins the amino acids together.
 Proteins result from the 20 amino acids ,
depending on the no.of amino acids and
sequence of amino acids.
 There are 4 levels of protein structure.

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Primary structure of protein
 Protein exists as a long chain of amino acids
arranged in a particular sequence.
 It is nonfunctional.
 Position of amino acid in a protein is obtain
from this.
 1st a. a is called N-terminal and last is called C-
terminal a. a.

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Secondary structure of
protein
 There is interaction between every fourth a. a
by formation of hydrogen bond. The
polypeptide has a helical shape. E.g. keratin.
 Only right handed helix are formed.
 If two or more chains are held together by
intermolecular hydrogen bonds, the structure
is called pleated sheet. E.g. silk fibres.

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Tertiary structure of
protein

 When a polypeptide chain becomes further


stabilised by folding and coiling by the
formation of ionic or hydrophobic bonds or
disulphide bridges, the protein is said to be
tertiary structure.
 E.g. amylase, pepsin and other enzymes.

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Quaternary structure of
protein

 When a protein has many sub units, each


having primary, sec. And tertiary st. of its own,
the protein is said to be quaternary.
 E.g. haemoglobin, insulin

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Enzymes
 They are proteins that catalyse biochemical
reaction, so called biocatalysts.
 Specific for their substrate.
 Each enzyme require a specific (optimum) pH &
temp.
 Accelerate a reaction by reducing the activation
energy.

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Nomenclature of enzyme
 Named by adding the suffix ‘ase’ to the substrate.
E.g. sucrase
 According to the physiological activity it
catalyses. E.g. oxidase, dehydrogenase
 The source from which they are obtained.
E.g.papain from papaya.

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Classification of enzyme
 Oxidoreductase
 Transferase
 Hydrolases
 Lyases
 Isomerasees
 ligases

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Mechanism of enzyme
action
 Three dimensional structure of enzyme has one
or more active site where the substrate binds.
 Active site acts as ‘ lock’ into which substrate fits
in like a ‘key’.
 The point where substrate binds is called
‘substrate binding site’.
 Substrate binding causes lowering of activation
energy & reaction to proceed at a faster rate.
 Binding of substrate induces the enzyme to alter
its shape and fit more tightly.
 Breaking of chemical bond of substrate and
formation of E-P complex.
 Enzyme releases product and free enzyme take
up another molecule.
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Activation energy requirement
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Factors affecting enzyme
action
 Temperature
 pH
 Substrate concentration
 chemicals

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Vmax

velocity

(s)
Effect of substrate BIOMOLECULES-CLASS
concentration XI BIOLOGY 24

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