Bio Chemistry Chapter # 3 Proteins
Bio Chemistry Chapter # 3 Proteins
Bio Chemistry Chapter # 3 Proteins
PROTEINS
Protein is derived from Greek Word “Proteious or Protos” which means First rank order or the
supreme.
• DNA replication
• Responding to stimuli
Definition:
Proteins are nitrogenous compound made up of various amino acids linked by “Peptide bond”
“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
Protein obtained from animal source is known as First Class Proteins which contains all essential
Amino Acids.
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.
(ii) Aliphatic Amino acid (Glycine, Alanine, Valine, Lucien, Iso-leucien, Proline, Methionine)
(i) Polar uncharged Amino Acid (Serine, Threonine, Cysteine, Asparagine, Glutamine)
(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).
• Must be taken through diet. These are histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan and valine.
• Not to be needed through diet. These are alanine, arginine, asparagine, aspartic
acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine.
• 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.
Classification of 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.
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK
(vii) Albuminoid
These are fibrous proteins. These include keratin, collagen and elastin.
On hydrolysis these proteins yield amino acids and other organic and inorganic components.
These are of the following types.
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.
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.
These are obtained by hydrolysis of conjugated proteins. E.g. Proteases, peptones and
oligopeptides
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
These proteins regulate most of the body metabolism. E.g. Hormones like insulin, glucagon,
growth hormones etc.
These proteins are responsible to give stability to the body. E.g. Keratin, collagen, Elastin etc
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.
These proteins help in contraction and relaxation in muscle E.g. Actin, myosin and tubulin
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).
BIOCHEMISTRY NOTES CHAPTER PROTEIN CHASMHA INSTITUTE OF MEDICAL SCIENCE DIK
Structure of Antibody
These proteins are the thread like structure. They are insoluble in water and high resistant to
enzyme digestion. Examples: Collagen, Elastin, Keratins etc.
• The primary structure of a protein consists of linear sequence of the amino acid along the
polypeptide chain.
• Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the
protein its 3-D shape.
• 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.
• 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