STAMFORD UNIVERSITY

BANGLADESH
Assignment
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 Introduction
1.Amino acids are building blocks of proteins
2.Proteins are composed of 20 different
amino acids.
3.Their chemical structure influences three
dimensional structure of protein.
4.They are important intermediates in
metabolism.
5.They can have hormonal and catalytic
function.
 Definition
An organic compound containing an
amino group (NH2 ),a carboxylic acid
group(COOH),and any of various side
groups, especially any of 20
compounds that have the basic
formula NH2CHRCOOH,and that link
together by peptide bonds to form
proteins or that function as chemical
messengers and as intermediates in
metabolism.
Classification of amino acid
On the basis of R group the most helpful
point is to separate amino acids into:
1.Non-polar((Hydrophobic)
a. Aliphatic side chain
b. Aromatic side chain
2.Polar(Hydrophilic)
a. Positively charged R group
b. Negatively charged R group
c. Un-charged R group
1. Non-polar amino acids:
a. Only carbon and hydrogen in their
side chain
b. Generally unreactive.
c. Determining 3-D structure of proteins

Glycine is the simplest amino acid having

single H atom as its side chain
Alanine, Valine, Leucine and Isoleucine
have saturated hydrocarbon R groups.
Leucine and Isoleucine are isomers of
each other.
Proline is rather an amino acid than
amino acid because its side chain is
bonded to the backbone Nitrogen as
well as to the alpha carbon
Phenylalanyl and Alanine with an extra
benzene group on the end side times
called phenyl group. Phenylalanine is
Tryptophan is highly hydrophobic and
structurally related to alanine but with
2 ring Indole group added in the place
of the single aromatic ring found in
phenylalanine
Polar hydrophilic R- group:
polar, uncharged R groups
Tyrosine is polar, very weakly acidic
phenylalanine with an extra OH
group
Serine and Threonine play important
role in enzymes which regulate
phosphorylation and energy
metabolism.
 Cysteine has Sulphur containing side group . It
tends to be more reactive. It is not very polar.
Asparagine and Glutamine are amide derivatives
of Aspartate(Aspartic acid)and
Glutamine(Glutamic acid)
Negatively charged R group:
Two amino acids with negatively charged side
chains Aspartate (Aspartic acid) and
Glutamate(glutamic acid)
They confirm a-ve charge on the protein of which
they are a part.
Positively charged R group:
Lysine and Arginine are positively
charged at neutral ph.
Histidine can be uncharged or
positively charged depending on its
local environment. It has important
role in catalytic mechanism of
enzymes.
 Classification based on chemical
constitution
Small amino acids : Glycine and Alanine
Branched amino acids : Valine ,Leucine and
Isoleucine
Hydroxyl amino acids : Serine and Threonine
Sulphur amino acids : Cysteine and Methionine
Aromatic amino acids : Phenylaline , Tyrosine and
Tryptophan
Acidic amino acid and their derivatives
:Glutamate , Glutamine
Basic amino acids : Lysine , Arginine and Histidine
 Essential amino acid
Required in diet
They must come from food or amino acid supplements
1.Isoleucine
2.Leucine
3.Lysine
4.Methionine
5.Phenylalanine
6.Threonine
7.Tryptophan
8.Valine

Food source : Fish ,meat , poultry-cottage cheese ,peanuts-lentils

Branched-chain amino acids all import ants in muscle.
 Non-essential amino acid
Required in diet.
The body can make these amino acids from the above essential amino acids.

1.Alanine
2.Arginine
3.Asparagine
4.Aspertic acid
5.Cystein
6.Glutamic acid
7.Glutamine
8.Glycine
9.Histidine
10.Proline
11.Serine
12.Tyrosine

These are essential for infants , since their bodies can not produce them yet.