Unit - 4 Proteins
Unit - 4 Proteins
Unit - 4 Proteins
proteins
Proteins
Proteins are polymers of amino acids
Proteins possess certain unique properties because of their giant size.
Proteins are classified into
Simple proteins, Conjugated proteins and Derived proteins
Simple proteins : Proteins which yield only amino acids or their derivatives on hydrolysis.
a) Albumins: Soluble in pure water and coagulable by heat. Eg: serum albumin, egg albumin
b) Globulins: Insoluble in pure water but soluble in NaCl solutions Eg: serum albumin (in
blood), tuberin (in potato) arachin and conarchin (in peanuts)
c) Glutelins: Insoluble in all neutral solvents but soluble in very dilute alkalies pure water but
soluble in NaCl solutions Eg: serum albumin (in blood), tuberin (in potato) arachin and
conarchin (in peanuts)
d) Prolamins: Soluble in 70 % alcohol Eg: gliadin (in wheat) and zein (in maize)
e) Prolamins: Soluble in water and insoluble in very dilute ammonia. On hydrolysis, they
give several amino acids among which the basic one predominate. Eg: thymus histones and
the globin of haemoglobin.
e) Protamins: Strongly basic proteins with low molecular weight are soluble in water, not
coagulable by heat and on hydrolysis yield large amount of basic amino acids Eg: Salmine
from salmine sperm.
Conjugated proteins : Hydrolysis of conjugated proteins yield α-amino acids and a non-
protein material.
The non-protein material is known as prosthetic group. On the basis of the prosthetic groups
present in the protein, they are classified in the following manner
Characteristics of proteins
Proteins are complex nitrogenous compounds
They are very important for body growth and are of prime importance.
They have very high molecular weights
They are considered as polypeptides with molecular weight above 10,000.
Proteins are colloidal in nature
Proteins are amphoteric because their molecules contain both acidic and basic groups.
Depending on the pH of the medium they exist as cations or anions and in the
presence of electric field, they move towards either to the cathode or anode
(electrophoresis)
Characteristics of proteins
At a particular pH, which is characteristic for each protein, the positive and negative
charges are balanced exactly and the protein molecule carries no net charge. This is called the
isoelectric point of the protein and at this point the protein molecule will not migrate in an
electric field. At this pH, the protein molecule is easily precipitated
All proteins are optically active
Proteins may be coagulated. This irreversible precipitation of protein is called denaturation.
This can be brought about by heat, strong acids or bases or various other agents as a result
of denaturation, the protein undergoes changes physically and chemically. Solubility,
molecular shape and size, biological activity of the protein may change.
The optical rotation of many proteins changes as a result of denaturation. Denaturation
involves changes in the secondary structure of the protein.
Proteins on hydrolysis yield amino acids. This hydrolysis may be brought about by acids,
alkalies or enzymes. Enzymic hydrolyis takes very long time.
Colour Reactions of proteins
1) Biuert Test: Copper sulphate + alkaline solution of a protein gives violet or red colour
2) Millon’s Test: Mercuric nitrate in nitric acid containing a traces of nitrous acid is
called Millon’s reagent.
Millon’s reagent + Protein solution , white precipitate is formed and slowly turns to pink
3) Xanthoproteic Test: Protein solution + conc.nitirc acid , yellow colour is produced
4) Ninhydrin Test: Protein in pyridine + ninhydrin, a deep blue to violet, pink or even
red colour is produced
Haemoglobin, a protein in the blood serves as an oxygen carrier to transport oxygen from
the lungs to the various tissues.
Another protein,actomyosin participates in muscular contraction
The hormone insulin produced in the pancreas controls sugar metabolism in the body
Nucleoproteins, conjugated proteins composed of substances called nucleic acids and
simple proteins are the main constituents of genes, the carriers of heredity
Antibodies, which are proteins, function to protect human beings against diseases
Proteins present in hair and finger nails serve as important structural elements of the
body
Structure of proteins
Primary Structure
CH3 CH3
Glycylalanine (gly-ala)- The main mode of linkage of the amino acid in proteins is the
peptide bond formed by the reaction of the carboxyl group of one amino acid with amino
group of another.
Primary structure of proteins: deals with the actual arrangement or sequence of various
amino acids held together by peptide lin
Limitations : It fails to throw light on the shape, configuration and conformation of the
molecule.
(a) If peptide bond is formed by two amino acids, there are two possible sequences
(2! = 1 x 2 = 2)
Eg: glycine and alanine gives two possible sequences
1) Glyclalanine (gly-ala)
2) Alanyl glycine (ala-gly)
(b) If peptide bond is formed by three amino acids, there are six possible sequences
(3! = 1 x 2 x 3 = 6)
Eg: glycine , alanine and leucine gives six possible sequences
1) Ala-gly-leu
2) Ala-leu-gly
3) Gly-ala-leu
4) Gly-leu-ala
5) Leu-ala-gly
6) Leu-gly-ala
(c) If there are “n” amino acids in a protein, they give rise to n! (n! = 1 x 2 x3
x4……n)sequences
Secondary structure of proteins: deals with the shape in which the long amino acid chain
exists, the way in which theprotein chain is folded and the nature of the bonds.
The proteins are globular proteins, indicate a coiled structure I which peptide bonds are
folded in a regular manner.
Folding occurs as a result of linking of the carboxyl and amide groups of the peptide chain
by means of hydrogen bonds. Such foldings produced or maintained by hydrogen bonding is
called secondary structure of proteins.
Evidences: In many proteins the hydrogen bonding produces a regular coiled arrangements
called α-helix. This secondary structure has been confirmed by
X-ray studies
Tertiary structure of proteins: deals with the way in which the polypeptide chains fold up
into various shapes. i.e globular or ellipsoidal.
This folding involves hydrogen bonding, ionic and disulphide bonds.
Tertiary structure is determined by temperature and pH.
Secondary structure of proteins
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