Unit - 4 Proteins

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UNIT IV

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.

Based on their solubility proteins are furhter classified into

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

No. Conjugated protein Prosthetic Example


group
1 Nucleoproteins Nucleic acid Yeast, Chromosomes
2 Glycoproteins Carbohydrate Mucin, Egg white
3 Phosphoproteins Phosphorus Caseinogen, Ovovitelin
4 Haemoproteins Heme Haemoglobin, Myglobin
5 Lipoproteins Lipids Lipovitelins in eggs
6 Chromoproteins Fe, Mg, Cu Haemoglobin, Chlorophyll,
Cyanocuprin
Derived proteins. These are proteins derived from simple or conjugated proteins by
physical or chemical means. Examples are: denatured proteins and peptides.
Classification based on the shape of the molecule
1) Globular proteins: These protiens have spherical shape and they are soluble
2) Fibrous proteins:
Selero protiens are fibrous proteins.
They resemble long ribbons or fibres in nature.
They are insoluble
They are found in the tougher type of tissues such as keratins of skin, hair and
feathers.
The collagens of tendons, elastins of ligaments and silk fibroin belong to this class
They are insoluble in water and other common solvents

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

Biological functions of proteins


Proteins are intimately connected with all the physical and chemical activities that
constitute life.
Some proteins called enzyme serve as catalysts to speed up the variety of chemical
transformations which living cells are able to accomplish
Other proteins function as hormones whose main activity is to control processes which
occur in living things. Eg: growth hormone produced by the pituitary gland
Biological functions of proteins

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

NH2 - CH2 - COOH NH2 - CH - COOH NH2 - CH2 - CO - NH - CH - COOH H20


glycine alanine

N-terminal Peptide link C-terminal

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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