Protein

Protein,
- any of a large number of organic compounds that
make up living organisms and are essential to
their functioning. First discovered in 1838,
proteins are now recognized as the predominant
ingredients of cells, making up more than 50
percent of the dry weight of animals.
Protein
- derived from the Greek word Proteios which
means “first”.
- 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
Proteins – are long chains of amino acids liked
together by peptide (amide) bond with positively
charge nitrogen containing amino group at one end
and a negatively charged carboxyl group at the other
end.

- are made up of 20 amino acids in different

sequences and numbers.
Amino acids – are organic acid containing an
amino (-NH2) group and carboxylic acid (-
COOH) group, and a hydrogen (H) atom
attached to carbon located next to the – COOH
group.

- the “building blocks of protein”

General formula of amino acid
• Humans have an estimated 30,000 different
proteins, of which only about 2 percent have
been adequately described. Proteins in the diet
serve primarily to build and maintain cells, but
their chemical breakdown also provides energy,
yielding close to the same 4 calories per gram
as do carbohydrates (see Metabolism).
• Besides their function in growth and cell
maintenance, proteins are also responsible for
muscle contraction. The digestive enzymes are
proteins, as are insulin and most other hormones.
The antibodies of the immune system are proteins,
and proteins such as hemoglobin carry vital
substances throughout the body.
• The major fibrous proteins, described below, are
collagen, keratin, fibrinogen, and muscle proteins.
• Protein molecules range from the long,
insoluble fibers that make up connective tissue
and hair to the compact, soluble globules that
can pass through cell membranes and set off
metabolic reactions. They are all large
molecules, ranging in molecular weight from a
few thousand to more than a million, and they
are specific for each species and for each organ
of each species..
 Structure of Proteins
The most basic level of protein structure, called the primary
structure, is the linear sequence of amino acids. Different
sequences of the acids along a chain, however, affect the
structure of a protein molecule in different ways. Forces such as
hydrogen bonds, disulfide bridges, attractions between positive
and negative charges, and hydrophobic (“water-fearing”) and
hydrophilic (“water-loving”) linkages cause a protein molecule
to coil or fold into a secondary structure, examples of which
are the so-called alpha helix and the beta pleated sheet.
When forces cause the molecule to become even
more compact, as in globular proteins, a tertiary
protein structure is formed. When a protein is made
up of more than one polypeptide chain, as in
hemoglobin and some enzymes, it is said to have a
quaternary structure.
Biological Importance of Protein
1. Proteins are present in all living tissues
as building blocks or structural
elements/components of 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.
8. Structural proteins provide mechanical
support to body.
9. Proteins as molecular receptors.
10. Carrier/transport proteins.
11. Storage proteins.
12. Proteins as constituents of respiratory
pigments.
13. Proteins factors involved in blood clotting.
14. Proteins maintain homeostasis.

Enzyme – Organic substances composed

of polymers of amino acids that act as
catalysts to regulate the speed of the many
chemical reactions involved in the
metabolism of living organisms.
Hormone (from Greek ὁρμή "impetus")
- often described as the body’s chemical
messengers, hormones regulate growth and
development, control the function of
various tissues, support reproductive
functions, and regulate metabolism
CLASSIFICATION OF PROTEINS
Proteins are broadly classified into three groups:
A. Simple Proteins – are proteins which is
complete. Compound hydrolyses into amino acids
and does not possess non protein molecule.
1. Albumins 5. Protamines
2. Globulins 6. Histones
3. Glutelins 7. Scleroproteins
4. Prolamines - Keratins
- Collagens
- Elastins
The major fibrous proteins, described below, are
collagen, keratin, fibrinogen, and muscle
proteins.
• Collagen, which makes up bone, skin, tendons, and cartilage,
is the most abundant protein found in vertebrates. The
molecule usually contains three very long polypeptide chains,
each with about 1000 amino acids, that twist into a regularly
repeating triple helix and give tendons and skin their great
tensile strength. When long collagen fibrils are denatured by
boiling, their chains are shortened to form gelatin.
• Keratin, which makes up the outermost layer of skin and
the hair, scales, hooves, nails, and feathers of animals,
twists into a regularly repeating coil called an alpha helix.
Serving to protect the body against the environment,
keratin is completely insoluble in water. Its many disulfide
bonds make it an extremely stable protein, able to resist the
action of proteolytic (protein-hydrolyzing) enzymes. In
beauty treatments, human hair is set under a reducing
agent, such as thioglycol, to reduce the number of disulfide
bonds, which are then restored when the hair is exposed to
oxygen.
• Fibrinogen is a blood plasma protein responsible
for blood clotting. With the catalytic action of
thrombin, fibrinogen is converted into
molecules of the insoluble protein fibrin, which
link together to form clots.
• Myosin, the protein chiefly responsible for
muscle contraction, combines with actin,
another muscle protein, forming actomyosin, the
different filaments of which shorten, causing the
contracting action.
B. Conjugated Proteins are complexes of
simple proteins with nonprotein; the nonprotein
part is called prosthetic group; and the entire
molecule is known as Holoprotein.

Apoprotein + Prosthetic group Holoprotein

(protein part) (non-protein part)
1. Nucleoproteins
2. Mucoproteins/Proteoglycans
3. Glycoproteins
4. Chromoproteins
5. Phosphoproteins
6. Lipoproteins
7. Metalloproteins
C. Derived Proteins are produced from the
natural proteins by various physical and
chemical factors.
1. Proteans
2. Proteases
3. Peptones
4. Peptides
Amino acids – are organic acid containing an amino
(-NH2) group and carboxylic acid (-COOH) group,
and a hydrogen atom attached to carbon located next
to the – COOH group. Amino acids are organic
acids, in which a hydrogen has been substituted by
an amino (-NH2) group.
They are small biomolecules.
- The “building blocks of protein”

General formula:

H
NH2- C –COOH
R
Classifications of Amino Acids:
Neutral Amino acids – the largest group of amino
acids.

subdivisions:
Aliphatic amino acids (absence of benzene ring or
related structure)
- Glycine (Gly) - Leucine (Leu)
- Alanine (Ala) - Isoleucine (Ile)
- Valine (Val)
- Serine (ser)
- Threonine

Aromatic amino acids (hydroxyl is bonded to

phenol which is a strong acid)
- Serine (ser) - Histidine (His)
- Tryptophan (Trp) - Threonine (Thr)
Heterocyclic Amino acids
- Tryptophan (Trp)
- Histidine (His)

Imino acids
- Proline (Pro)
- Hydroxyproline (Hyp)
Sulfur Containing amino acids
- Cysteine (cys)
- Methionine (Met)

Acidic amino acids – consist of two –COOH group

and one –NH2 group.
- Aspartic acid (ASP)
- Asparagine (Asn)
- Glutamic acid (Glu)
Basic Amino acids – consist of one –COOH group
and two –NH2.

- Arginine (Arg.)
- Lysine (Lys)
- Hydroxylysine (Hyl)
Biological Importance of Amino acids:
1. Some amino acids are converted to carbohydrates
and are called as glycogenic amino acids.

2. Specific amino acids give rise to specialized

products – tyrosine forms thyroid hormones
• Tryptophan synthesizes a vitamin niacin.
• Glutamate, cysteine and glycin synthesize
glutathione an antioxidant.
• Lysine, arginine, methionine synthesize creatine.
• Glycine, cysteine help in synthesis of bile salts
• Several amino acids are used in purine and pyrimidine
biosynthesis (RNA & DNA).
• Cysteine and methionine are sources
of sulfur.
• Methionine acts as active methionine transfers
methyl group to various substances.
Amino acids may be:
Essential Amino Acids – are acids not synthesized
in the body but are very essential as constituents of
tissue proteins and hence required to be supplied in
food.
Nonessential Amino acids- can be synthesized in
the body, hence they are not essential to be supplied
in the diet.
Deficiency means
-protein synthesis do not occur and nitrogen
excretion is great leading to wasting of the
tissues.
Functions of essential amino acids:
1. Tryptophan: Necessary for the synthesis of
neurotransmitter serotonin. It helps relieve
migraine and depression.
2. Tyrosine: Is precursor of dopamine,
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 include
hallucinations.
4. Isoleucine: Necessary for the synthesis of
hemoglobin, major constituent of red blood cells.
5. Leucine: Beneficial for skin, bone and tissue
wound healing. It promotes growth hormone
synthesis.
6. Lysine: Component of muscle protein, and is
needed in the synthesis of enzymes and hormones. It
is also a precursor for L-carathine which is essential
for healthy nervous system function.
7. Methionine: Is antioxidant. It helps in breakdown
of fats and aids in reducing muscle degeneration. It
is also good for healthy skin and nail.
8. Phenylalanine: Beneficial for healthy nervous
system. It boosts memory and learning. It may be
useful against depression and suppressing appetite.
9. Asparagine: It helps promote equilibrium in the
central nervous system—aids in balancing 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.
To much Protein?
When we consume more protein than the
required amount:
1. cause excess nitrogen to be
excreted as urea in urine.
2. excess nitrogen linked to reduced
kidney function in later years.
3. lead to dehydration due to
excessive urine output.
4. Cause extra metabolic stress to be placed on
the liver.
5. Increases excretion of calcium
6. high protein diets linked to osteoporosis, and
calcium on its way through the urinary system
can produce kidney stones.
7. increased risk of inadequate vitamins and
minerals especially antioxidants,
low fiber intake, high total and saturated fat
intake, excess caloric intake, as well as excess
protein intake.

These imbalances carry with them long term

negative consequences.