BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

PROTEINS

Protein is derived from Greek Word “Proteious or Protos” which means First rank order or the
supreme.

• Proteins are large biomolecules, or macromolecules, consisting of one or more long

chains of amino acid residues.

• Proteins perform a vast array of functions within organisms, including

• Catalyzing metabolic reactions

• DNA replication

• Responding to stimuli

• Providing structure to cells, and organisms

• Transporting molecules from one location to another.

 Definition:

Proteins are nitrogenous compound made up of various amino acids linked by “Peptide bond”

Protein can be defined as;

“Any of various naturally occurring complex substances that consist of amino-acid residues
joined by peptide bonds, contain the elements carbon, hydrogen, nitrogen, oxygen, usually
sulfur, and occasionally other elements (such as phosphorus or iron), and include many essential
biological compounds (such as enzymes, hormones, or antibodies)”.

 Sources of Proteins

Animal Sources: Meat, Fish, Egg etc.

Protein obtained from animal source is known as First Class Proteins which contains all essential
Amino Acids.

Plant sources: Pulses, Legumes, Wheat etc.

Protein obtained from plant source is known as Second Class Proteins which do not contains all
essential Amino Acids.
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

 Amino Acid

Amino acids are the basic structural unit of proteins. Amino acids are organic compounds that
contain amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R
group) specific to each amino acid. About 300 naturally occurring amino acids are known
(though only 20 appears in the formation of protein).

The key elements of an amino acid are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N),
although other elements are found in the side chains of certain amino acids.

 Classification of Amino Acids on the basis of Polarity

(i) Non Polar Amino Acid

(i) Aromatic Amino acid (Phenylalanine, Tryptophan, Tyrosine)

(ii) Aliphatic Amino acid (Glycine, Alanine, Valine, Lucien, Iso-leucien, Proline, Methionine)

(ii) Polar Amino Acid

(i) Polar uncharged Amino Acid (Serine, Threonine, Cysteine, Asparagine, Glutamine)

(ii) Polar charged Amino Acid

(a) Positively charged Amino Acid or Basic Amino acid (Lysine, Histidine, Arginine)

(b) Negatively charged Amino Acid or Acidic Amino acid (Aspartic Acid, Glutamic Acid).

 Classification of Amino Acids on the basis of participation in protein synthesis

• (i) Standard Amino Acid (20 Amino acid).

BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

• Those amino acids which can take part in synthesis of proteins.

• (ii) Non-Standard Amino Acid

• Those amino acids which do not take part in synthesis of proteins.

 Classification of Amino Acids on the basis of nutrition

• (i) Essential Amino Acid

• Must be taken through diet. These are histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan and valine.

• (ii) Non-Essential Amino Acid

• Not to be needed through diet. These are alanine, arginine, asparagine, aspartic
acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine.

• (iii) Semi-Essential Amino Acid

• Synthesized naturally in the body but these are not enough in amount to take part in a
reaction. Therefore these amino acids are also taken through diet such as Arginine,
Histidine.

 Peptide Bond

• A covalent bond formed by joining the carboxyl group (COOH) of one amino acid to the
amino group (NH2) of another amino acid, with the removal of a molecule of water. The
process of removal of water is known as condensation.

• When many peptides are combined, it forms polypeptide chain.

BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

 Formation of peptide bond between different Amino Acids

 Structures of Non-Polar, Polar Uncharged & Polar charged Amino Acid

 Classification of Proteins
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

 Classification of proteins

Proteins can be classified as below.

(1) Physio-chemical classification

These include simple protein, compound proteins and derived proteins.

(a) Simple proteins

These proteins contain only amino acids and have no Non-protein component. On hydrolysis
they can yield only amino acids and no other major organic or inorganic hydrolysis products.

(i) Albumin

These are synthesized only in liver. These simple proteins are soluble in water. These simple
proteins are coagulated by heat. Examples are serum albumin, egg albumin etc

(ii) Globulin

These proteins are present in serum, muscle and other tissues. These simple proteins are
synthesized in liver and spleen. These simple proteins are soluble in dilute salt solution but
readily in water.

(iii) Globin

Globin is the protein part of hemoglobin. Globin unites with heme to form hemoglobin. Rich in
Histidine (Basic AA).

(iv) Prolamines

These are simple proteins and these are rich in the amino acid proline. e.g. =Gliadin of wheat

(v) Histones

Histones are Simple proteins. They contain basic amino acids like Arginine, Lysine and
Histidine Histones combine with DNA and form nucleoprotein.

(vi) Protamine

These are basic proteins because protamines are rich in Arginine. They combine with DNA and
form nucleoprotein. These are present in sperm cells.
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(vii) Albuminoid

These are fibrous proteins. These include keratin, collagen and elastin.

(b) Conjugated Protein

On hydrolysis these proteins yield amino acids and other organic and inorganic components.
These are of the following types.

(i) Nucleoprotein: A protein containing nucleic acid.

(ii) Lipoprotein: A protein containing lipid
(iii) Phosphoprotein: A protein containing phosphorous
(iv) Metalloprotein: A protein containing metal ion.
(v) Glycoprotein: A protein containing carbohydrate.

(c) Derived proteins

These are the proteins which are derived from simple and conjugated proteins through heat, PH
change, enzyme or various chemical reactions, These includes primary derived protein and
secondary derived proteins.

(i) Primary derived proteins

These are denatured proteins. Denaturation is a process in which all the bonds present in protein
will break down. Denaturation can be done by changing the pH of protein, by heat, by chemical
factors like Acids and have, detergents, etc. These proteins are easily digestible.

(ii) Secondary derived proteins

These are obtained by hydrolysis of conjugated proteins. E.g. Proteases, peptones and
oligopeptides

(2) Functional Classification

On functional basis protein are classified as below.

(i) Catalytic protein

These proteins are responsible to speed up the chemical reactions occur inside the living body
e.g. Enzyme
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

(ii) Regulatory proteins

These proteins regulate most of the body metabolism. E.g. Hormones like insulin, glucagon,
growth hormones etc.

(iii) Structural protein

These proteins are responsible to give stability to the body. E.g. Keratin, collagen, Elastin etc

(iv) Transport proteins

These proteins are involved for the carry of different substance in the blood

E.g. Hemoglobin is a protein which is responsible to carry oxygen to different parts of the body.

(v) Contractile protein

These proteins help in contraction and relaxation in muscle E.g. Actin, myosin and tubulin

(vi) Storage protein

These store protein for nutritional purpose. E.g. ovalbumin

(vii) Respiratory Proteins

These proteins help in oxidative phosphorylation. E.g. cytochrome complex

(viii) Blood clotting factor proteins

These proteins help in Blood clotting. E.g. Fibrinogen

(ix) Defensive protein (Immune protein)

These proteins are responsible for immunity of the body against germs (antigen)

E.g. Antibody

Antibody

Each antibody molecule has Y shaped. It has three segments. Each antibody molecule has 2 light
chains and two heavy chains. The heavy chain and light chain are held together by disulphide
bond (S-S).
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Structure of Antibody

(3) Structural classification

They can be classified as

(i) Fibrous protein

These proteins are the thread like structure. They are insoluble in water and high resistant to
enzyme digestion. Examples: Collagen, Elastin, Keratins etc.

(ii) Globular Protein

These are somewhat rounded in shape. These are soluble in water

BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

(4) Classification of Protein on their level of organization

(i) Primary Structure

• The primary structure of a protein consists of linear sequence of the amino acid along the
polypeptide chain.

• Amino acids are joined by peptide bonds.

(ii) Secondary Structure

• Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the
protein its 3-D shape.

• There are two types of secondary structures observed in proteins.

• One type is the alpha (α) helix structure. This structure resembles a coiled spring and is
secured by hydrogen bonding in the polypeptide chain.

• The second type of secondary structure in proteins is the beta (β) pleated sheet. This
structure appears to be folded or pleated and is held together by hydrogen bonding
between polypeptide units of the folded chain that lie adjacent to one another.

(iii) Tertiary Structure

• Tertiary Structure refers to the comprehensive 3-D structure of the polypeptide chain of
a protein. There are several types of bonds and forces that hold a protein in its tertiary
structure. These are hydrophobic interactions, hydrogen bonding, ionic bonding and
disulfide bridge

(iv) Quaternary Structure

• Quaternary Structure refers to the structure of a protein macromolecule formed by

interactions between multiple polypeptide chains. Each polypeptide chain is referred to as
a subunit.
• Proteins with quaternary structure may consist of more than one of the same type of
protein subunit or may also be composed of different subunits.
• Hemoglobin is an example of a protein with quaternary structure. It contains four
subunits: two alpha subunits and two beta subunits.
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

 Clinical Significance of Protein

• Proteins are major source of energy. I gram of protein yields 4.1 Kcal.
• Fibrinogens are protenious in nature and involved in blood clotting.
• Enzyme (protein in nature) catalyzed various metabolic reactions in living bodies.
• Main integral component of cell membrane.
• Nucleoprotein serves as hereditary carrier agent from generation to generation.
• Receptors are proteins which can receive stimulus.
• Hormone regulates various mechanisms within the living organisms such as Insulin and
Glucagon regulate blood glucose level in humans.
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK

• Hemoglobin (an important protein) responsible of carries oxygen to various parts of

body.
• Defensive protein such as antibody protect living organism from various pathogens.
• Several structural proteins such as Keratin, Collagen, and Elastin etc. perform major role
in structural formation and provide strength to various organs.