PROTEIN Amino acids– are organic acid containing an

amino (-NH2) group and carboxylic acid

 any of a large number of organic
(- COOH) group, and a hydrogen
compounds that make up living
(H) atom attached to carbon located
organisms and are essential to their
next to the – COOH group.
functioning. First discovered in 1838,
 the “building blocks of protein”
proteins are now recognized as the
predominant ingredients of cells,
making up more than 50 percent of the General formula of amino acid
dry weight of animals.
 derived from the Greek word Proteios
which means “primary” by Dutch
chemist Gerard Johann Mulder (1838).
 by Swedish chemist Jons J. Berzelius
(1838) “first of the rank”.
 first among natural polymers essential
for growth and maintenance of life.
 contain N2, O2, C and H2
 also contain S, P, Cu, Zn and Fe

 MW ranging from 10,000 to several

millions.
 Obtained by condensation
polymerization of amino acids through
the formation of peptide bonds.

 Polymer= compound with repeating

small molecules.
 Polymerization= process of making
polymers: the chemical reaction in
which a compound is made into a
polymer by the addition or
condensation of smaller molecules.
 Humans have an estimated 30,000
different proteins, of which only about
Proteins– are long chains of amino acids liked 2 percent have been adequately
together by peptide (amide) bond with described. Proteins in the diet serve
positively charge nitrogen containing primarily to build and maintain cells,
amino group at one end and a but their chemical breakdown also
negatively charged carboxyl group at provides energy, yielding close to the
the other end. same 4 calories per gram as do
 are made up of 20 amino acids in carbohydrates (see Metabolism).
different sequences and  Besides their function in growth and cell
numbers. maintenance, proteins are also
responsible for muscle contraction. The
 digestive enzymes are proteins, as are enzymes, it is said to have a quaternary
insulin and most other hormones. The structure.
antibodies of the immune system are
proteins, and proteins such as
hemoglobin carry vital substances
throughout the body.
Biological Importance of Protein
1. Proteins are present in all living tissues
 The major fibrous proteins, described
as building blocks or structural,
below, are collagen, keratin, fibrinogen,
physiological elements/components of
and muscle proteins. the body.
2. Proteins are the essence of life
processes.
3. They are the fundamental constituents of
protoplasm and are involved in the
structure and functions of cells.
4. Proteins are important dietary
constituents for supply of nitrogen as
well as sulfur. Can be
catabolized to produce energy.
5. Enzymes are proteins.
6. Hormones are proteins.
7. Antibodies are proteins.
Structure of Proteins 8. Structural proteins provide mechanical
support to body.
9. Proteins as molecular receptors.
The most basic level of protein structure, called 10. Carrier/transport proteins.
the primary structure, is the linear sequence of 11. Storage proteins.
amino acids. Different sequences of the acids 12. Proteins as constituents of respiratory
along a chain, however, affect the structure of a pigments.
protein molecule in different ways. Forces such 13. Proteins factors involved in blood
as hydrogen bonds, disulfide bridges, clotting.
attractions between positive and negative 14. Proteins maintain homeostasis.
charges, and hydrophobic (“water-fearing”) and
hydrophilic (“water-loving”) linkages cause a Enzyme– Organic substances
protein molecule to coil or fold into a secondary composed of polymers of amino acids
structure, examples of which are the so-called that act as catalysts to regulate the speed
of the many chemical reactions involved
in the metabolism of living organisms.
alpha helix and the beta pleated sheet.
Hormone (from Greek ὁρμή
When forces cause the molecule to become "impetus")- often described as the
even more compact, as in globular proteins, a body’s chemical messengers, hormones
regulate growth and development,
tertiary protein structure is formed. When a
control the function of various tissues,
protein is made up of more than one
support reproductive functions, and
polypeptide chain, as in hemoglobin and some
regulate metabolism.
 which are then restored when the hair is
exposed to oxygen.
 Fibrinogen is a blood plasma protein
Classifications of Protein responsible for blood clotting. With the
Proteins are broadly classified into three groups: catalytic action of thrombin, fibrinogen
is converted into molecules of the
A. Simple Proteins – are proteins insoluble protein fibrin, which link
which is complete. Compound together to form clots.
hydrolyses into amino acids and  Myosin, the protein chiefly responsible
does not possess non protein for muscle contraction, combines with
molecule. actin, another muscle protein, forming
1. Albumins 5. Protamines actomyosin, the different filaments of
2. Globulins 6. Histones which shorten, causing the contracting
3. Glutelins action.
7.Scleroproteins
4. Prolamines B. Conjugated Proteins are complexes of
-Keratins simple proteins with nonprotein; the nonprotein
-Collagens part is called prosthetic group; and the entire
-Elastins molecule is known as Holoprotein.
The major fibrous proteins, described below,
Apoprotein + Prosthetic group
are collagen, keratin, fibrinogen, and
Holoprotein (protein part) (non-protein part)
muscle proteins.
 Collagen, which makes up bone, skin,
1. Nucleoproteins
tendons, and cartilage, is the most
2. Mucoproteins/Proteoglycans
abundant protein found in vertebrates.
3. Glycoproteins
The molecule usually contains three
4. Chromoproteins
very long polypeptide chains, each with
5. Phosphoproteins
about 1000 amino acids, that twist into a
6. Lipoproteins
regularly repeating triple helix and give
7. Metalloproteins
tendons and skin their great tensile
strength. When long collagen fibrils are
C. Derived Proteins are produced from the
denatured by boiling, their chains are
natural proteins by various physical and
shortened to form gelatin.
chemical factors.
 Keratin, which makes up the outermost 1. Proteans
layer of skin and the hair, scales, 2. Proteases
hooves, nails, and feathers of animals, 3. Peptones
twists into a regularly repeating coil 4. Peptides
called an alpha helix. Serving to protect Amino acids – are organic acid containing an
the body against the environment, amino (-NH2) group and carboxylic acid (-
keratin is completely insoluble in water. COOH) group, and a hydrogen atom attached to
Its many disulfide bonds make it an carbon located next to the – COOH group.
extremely stable protein, able to resist Amino acids are organic acids, in which a
the action of proteolytic (protein- hydrogen has been substituted by an amino (-
hydrolyzing) enzymes. In beauty NH2) group.
treatments, human hair is set under a They are small biomolecules.
reducing agent, such as thioglycol, to The “building blocks of protein”
reduce the number of disulfide bonds,
General formula:
H
NH2-C – COOH
Biological Importance of Amino
R
acids
Classifications of Amino Acids 1. Some amino acids are converted to
carbohydrates and are called as glycogenic
Neutral Amino acids – the largest group of amino acids.
amino acids. 2. Specific amino acids give rise to specialized
subdivisions: products – tyrosine forms thyroid hormones
Aliphatic amino acids (absence of benzene • Tryptophan synthesizes a vitamin niacin.
ring or related structure) • Glutamate, cysteine and glycin synthesize,
- Glycine (Gly) - glutathione an antioxidant.
Leucine (Leu) • Lysine, arginine, methionine synthesize
- Alanine (Ala) - creatine.
Isoleucine (Ile) • Glycine, cysteine help in synthesis of bile salts
- Valine (Val) - Serine (ser) • Several amino acids are used in purine and
- Threonine pyrimidine biosynthesis (RNA & DNA).
Aromatic amino acids (hydroxyl is bonded • Cysteine and methionine are sources of sulfur.
to phenol which is a strong acid) • Methionine acts as active methionine transfers
- Serine (ser) - Histidine methyl group to various substances.
(His)
- Tryptophan (Trp) - Threonine Amino acids may be:
(Thr) Essential Amino Acids– are acids not
Heterocyclic Amino acids synthesized in the body but are very essential as
- Tryptophan (Trp) constituents of tissue proteins and hence
- Histidine (His) required to be supplied in food.
Imino acids Non-essential Amino acids- can be
- Proline (Pro) synthesized in the body, hence they are not
- Hydroxyproline (Hyp) essential to be supplied in the diet.
Sulfur Containing amino acids
- Cysteine (cys) Deficiency means
- Methionine (Met)  protein synthesis do not occur and
Acidic amino acids – consist of two –COOH nitrogen excretion is great leading to
group and one –NH2 group. wasting of the tissues.
- Aspartic acid (ASP)
- Asparagine (Asn)
- Glutamic acid (Glu)
Functions of essential amino acids:
Basic Amino acids – consist of one –COOH 1. Tryptophan: Necessary for the synthesis of
group and two – NH2. neurotransmitter serotonin. It helps relieve
- Arginine (Arg.) migraine and depression.
- Lysine (Lys) 2. Tyrosine: Is precursor of dopamine,
- Hydroxylysine (Hyl) norepinephrine and adrenaline. It enhances
positive mood. It is also antioxidant.
3. Valine: Essential for muscle development.
Side effects of high levels of valine in the body To much Protein?
include hallucinations.
When we consume more protein than the
4. Isoleucine: Necessary for the synthesis of required amount:
hemoglobin, major constituent of red blood
cells. 1. cause excess nitrogen to be excreted as urea in
5. Leucine: Beneficial for skin, bone and tissue urine.
wound healing. It promotes growth hormone 2. excess nitrogen linked to reduced kidney
synthesis. function in later years.
6. Lysine: Component of muscle protein, and is 3. lead to dehydration due to excessive urine
needed in the synthesis of enzymes and output.
hormones. It is also a precursor for L-carathine 4. Cause extra metabolic stress to be placed on
which is essential for healthy nervous system the liver.
function. 5. Increases excretion of calcium
7. Methionine: Is antioxidant. It helps in 6. high protein diets linked to osteoporosis, and
breakdown of fats and aids in reducing muscle calcium on its way through the urinary
degeneration. It is also good for healthy skin and system can produce kidney stones.
nail. 7. increased risk of inadequate vitamins and
8. Phenylalanine: Beneficial for healthy minerals especially antioxidants, low fiber
nervous system. It boosts memory and learning. intake, high total and saturated fat intake, excess
It may be useful against depression and caloric intake, as well as excess protein intake.
suppressing appetite.
9. Asparagine: It helps promote equilibrium in These imbalances carry with them long term
the central nervous system—aids in balancing negative consequences.
state of emotion.
10. Proline: play role in intracellular signaling.
11. Aspartic acid: Enhances stamina, aids in
removal of toxins and ammonia from the body,
and beneficial in the synthesis of proteins
involved in the immune system.
12. L-arginine: plays role in blood vessel
relaxation, stimulating and maintaining erection
in men, production of ejaculate, and removal of
excess ammonia from the body.

ISOMERISM
Two types are exhibited by amino acids due to
the presence of asymmetric carbon.
All amino acids except Glycine, exist in D and L
forms.

L – amino acids, when

• -NH2 group is on the left of the a-
carbon or written below.
• -COOH is on top or –COOH to
the right of the a-carbon.