Amino Acid Peptides and

Proteins
Madhusmita Roy
M.Sc. MLST
Moderator
Dr.Garima Chauhan
Amino Acid
Amino acids are a group of organic compounds
containing two functional groups- amino and
carboxyl. The amino group(-NH2) is basic while
the carboxyl group(-COOH) is acidic in nature.
There are 20 common alpha amino acids used
by the ribosomes to make proteins.
Classification of Amino Acids
A. Classification based on the structure
 Amino acids with Aliphatic side chain: Glycine ,
Alanine , Valine , Leucine , Isoleucine.
 Amino acids with Hydroxyl groups(-OH) : Serine ,

Threonine , Tyrosine
 Amino acids with Sulfur group: Cysteine ,

Methionine
 Acidic Amino acids and their amides: Aspartic

Acid , Asparagine , Glutamic Acid , Glutamine

 Basic Amino Acids: Lysine , Arginine , Histidine

 Aromatic Amino Acids: Phenylalanine , Tyrosine ,

Tryptophan
 Imino Acid: Proline
B. Classification based on polarity
 Non- Polar Amino Acids: These Amino acids

are hydrophobic and they have no charge

on their ‘R’ group. They are Alanine ,
Leucine , Isoleucine , Valine , Methionine ,
Tryptophan , Phenyl-alanine and Proline.
 Polar amino acids with no charge on ‘R’

group: Glycine , Serine , Threonine ,

Glutamine , Asparagine , Cysteine , Tyrosine
 Polar amino acids with positive ‘R’ group:

Lysine , Arginine , Histidine

 Polar amino acids with negative ‘R’ group:

Aspartic Acid and Glutamic Acid

C. Nutritional classification of amino acids:
 Essential Amino acids: The amino acids which cannot be
synthesized by our body and therefore need to be
supplied through the diet called essential amino acids.
They are required for the proper growth and maintenance
of the individual. The ten amino acids are – Arginine ,
Valine , Histidine , Isoleucine , Leucine , Lysine ,
Methionine , Proline , Threonine , Tryptophan.
 Semi- essential Amino acids: The two amino acids namely
Arginine and Histidine can be synthesized by adults and
not by growing children. Hence it is called Semi-essential
amino acids.
 Non-essential Amino acids: The body can synthesize 10
amino acids to meet the biological needs , hence they
need not be consumed in their diet. These are- Glycine ,
Alanine , Serine , Cysteine , Aspartate , Asparagine ,
Glutamate , Glutamine , Tyrosine , and Proline.
D. Classification based on metabolic fate:
 Glycogenic Amino Acids: Alanine , Aspartate

, Glycine etc.
 Ketogenic Amino Acids: Lysine and Leucine
 Glycogenic and Ketogenic Amino Acids:

Isoleucine , Phenyl-alanine , Tyrosine , and

Tryptophan.
Amino Acids useful as drugs
There are some non-standard amino acids that
are used as drugs.
o D-Penicillamine a metabolite of penicillin, is

employed in the chelation therapy Wilson’s

disease.
o N-Acetyl cysteine is used in cystic fibrosis,

and chronic renal insufficiency , as it can

function as an anti-oxidant.
o Gabapentin is used as an anti convulsant.
Peptide Bond
 Amino Acids are joined
together covalently by
peptide linkage which
is amide linkage
between the carboxyl
group carboxyl group
of one amino acids and
the alpha amino group
of other.
 The peptide bonds are
not broken by high
conditions like heat
that denature proteins.
Characteristics of Peptide Bond

 Exists in resonating form

 Shows partial double bond character
 Shorter than the normal C-N bond
 Uncharged but polar
 No free rotation around the bond
Peptides and Polypeptides
 Peptides are chains of Amino Acids.
 Three Amino acids can join by two peptide

bonds to form a Tripeptide.

 When few amino acids are joined together by

peptide bonds, the structure is called an

Oligopeptide.
 When many amino acids are joined together

is , the product is called a Polypeptide.

Proteins
 Protein:Greek word:proteios-holding the first
place.
 Proteins are linear unbranched polymers

constructed from 22 standard amino acids

that are encoded in the DNA of the genome.
 Final product of information pathway-

DNA-------RNA--------PROTEIN
 The fundamental units of protein polymers

are alpha amino acids.

Structure of Proteins
Structure of protein is rather complex and can be
studied under four organizations:
1. Primary Structure: The linear sequence of amino
acids forming the backbone of proteins
(polypeptides).
2. Secondary Structure: The spatial configuration of
the protein by twisting the polypeptide chain.
3. Tertiary Structure: The three dimensional structure
of a functional protein.
4. Quaternary Structure: Some of the proteins are
composed of two or more polypeptide chains
referred to as subunits. The spatial arrangement
of these subunit is known as quaternary structure.
Classification of Proteins
A. Functional Classification
 Structural Proteins : Keratin of hair , and nails
 Enzymes or Catalytic Proteins: Hexokinase , Pepsin
etc.
 Transport Proteins: Hemoglobin , Serum albumin
 Hormonal proteins: Insulin , Growth hormone.
 Contractile Proteins: Actin , Myosin
 Storage Proteins: Ovalbumin , glutelin
 Genetic Proteins: Nucleoprotein
 Defense Proteins: Snake venoms and
immunoglobulin
B. Classification based on structure and solubility
 Simple Protein: composed only of amino acid

residues.
a) Simple Protein- e.g. Albumin, globulin
b) Fibrous Protein- e.g. Collagen , elastin etc.
 Conjugated Protein: contains non protein

moieties(prosthetic group) besides amino

acids.
e.g. metalloproteins (e.g. Cerulloplasmin),
Chromoproteins(e.g. Hemoglobin)
 Derived Protein: denatured or degraded

products of simple and conjugated proteins.

e.g. coagulated proteins( by heats , acids etc.)
peptones , polypeptides etc.
C.Nutritional Classification of
Proteins
 Complete Proteins: contain all essential 10
amino acids.e.g. milk casein, egg albumin
etc.
 Partially complete proteins: partially lack one
or more essential amino acids e.g. wheat and
rice proteins(partially lack Lysine and
threonine)
 Incomplete proteins: completely lack one or
more essential amino acids. Hence can’t
promote growth at all. E.g. gelatin
FUNCTIONS OF
PROTEINS