21BTB102T - UNIT III

Proteins

Proteins are a class of organic compounds consisting almost entirely of carbon, hydrogen,
oxygen, and nitrogen. The protein is actually a polymer composed of many subunits (monomers)
known as amino acids.

The amino acids usually found in proteins show the following structure:

The COOH (carboxyl) group is characteristic of all organic acids and is attached to the
same carbon as the NH2 group.

This carbon is designated the α-carbon atom; the entire amino acid is known as α-amino
acid. The R is a general designation for a variety of side groups that differentiate the 20
different amino acids found in nature, as shown in Figure.

Such properties of a protein as its water solubility or charge are due to the kinds of R
groups found in its constituent amino acids. In a manner similar to the way
monosaccharides join to form higher-order polysaccharides, amino acids join by
expelling a molecule of water.

An_OH is removed from the carboxyl group of one amino acid, and a _H is removed
from the amino group of a second. The resultant bond between the C and N atoms of the
carboxyl and amino groups is called a peptide bond, and the compound formed is a
dipeptide.

A dipeptide may unite with another amino acid to form a second peptide bond, and this
will yield a tripeptide. If many amino acids are joined in this condensation process, the
result is a polypeptide; such chains of amino acids may range from less than 100 amino
acids to as many as 1000.

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Classification of Proteins

Classification of proteins is done on the basis of the following:

• Shape

• Constitution

• Nature of molecules
I. On the basis of shape

• Fibrous protein(Scleroprotein): We can find these proteins in animals and are insoluble in water.
Fibrous proteins are resistant to proteolytic enzymes and are coiled and exist in threadlike structures to
form fibres. e.g. collagen, actin, and myosin, keratin in hair, claws, feathers, etc.

• Globular proteins: These proteins, unlike fibrous proteins are soluble in water. They are made up of
polypeptides that are coiled about themselves to form oval or spherical molecules e.g. albumin,
insulin, and hormones like oxytocin, etc.
II. On the basis of Constitution

• Simple proteins: These proteins are made up of amino acids only. e.g. albumins, globulins,
prolamins, etc.

• Conjugated proteins: These are complex proteins that are combined with the characteristic of non–
amino acid substance called as a prosthetic group. These are of following types:–

o Nucleoproteins: Combination of protein and nucleic acid

o Mucoproteins: Combination of proteins and carbohydrates (>4%)

o Glycoproteins: Combination of proteins and carbohydrates(<4%)

o Chromoproteins: Combination of proteins and coloured pigments.

o Lipoproteins: Combination of proteins and lipids.

o Metalloprotein: Combination of proteins and metal ions.

o Phosphoprotein: Combination of proteins and phosphate group.

• Derived proteins: When proteins are hydrolyzed by acids, alkalies or enzymes, the degradation
products obtained from them are called derived proteins.

III. On the basis of nature of Molecules

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 • Acidic proteins: They exist as anion and contain acidic amino acids. e.g. blood groups.

• Basic proteins: They exist as cations and are rich in basic amino acids e.g. lysine, arginine etc.

Functional Classification of Proteins

• Enzymes (biochemical catalysts)-In living organisms, almost all reactions are catalyzed by specific
proteins called enzymes. They have a high catalytic power, increasing the rate of the reaction in
which they are involved at least by factor 106. Eg: Glucose isomerase

• Transport proteins -Many small molecules, organic and inorganic, are transported in the
bloodstream and extracellular fluids, across the cell membranes, Eg: hemoglobin, that carries
oxygen from the alveolar blood vessels to tissue capillaries;

• Storage proteins-Examples are: ferritin, that stores iron intracellularly in a non-toxic form

• Mechanical support-Proteins have a pivotal role in the stabilization of many structures. Examples
are α-keratins, collagen and elastin.

• Movement-Example-the contraction of the muscle fibers (of which myosin is the main component);

• Nerve transmission.-An example is the receptor for acetylcholine at synapses.

• Hormones- regulatory functions Example is insulin,

• Protection against harmful agents.-The antibodies or immunoglobulins are glycoproteins that

recognize antigens expressed on the surface of viruses, bacteria and other infectious agents.

• Storage of energy-Proteins in particular the amino acids that constitute them, act as energy storage,
second in size only to the adipose tissue, that in particular conditions, such as prolonged fasting,
may become essential for survival.

STRUCTURE OF PROTEINS

Primary structure: The linear polpeptide chain of amino acids in a protein establishes its primary
structure. This primary structure is actually encoded in the genetic blueprint that ispreserved and
passed on from parent to child in the DNA of the chromosomes.

Structure of Proteins

Primary Structure

• The linear polpeptide chain of amino acids in a protein establishes its primary
structure. This primary structure is actually encoded in the genetic blueprint that is

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 preserved and passed on from parent to child in the DNA of the chromosomes.

Secondary Structure

• The interactions between the bonded amino acids of the primary structure may lead to
folding, kinking, or even pleating of the protein chain.
• Hydrogen bonding is largely responsible for these changes in the configuration of the
protein chain, which constitute the secondary structure of the protein molecule.
• Among the shapes assumed in secondary structure is the αhelix—a configuration similar
to a winding staircase or stretched spiral. Another kind of secondary structure is the Beta
pleated sheet.

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Tertiary Structure

• Superimposed on the secondary structure may be striking alterations, consisting of

superfolding or a complex twisting that yields highly intricate spheres or globules, in the
three-dimensional shape of the molecule. This constitutes the tertiary structure of a
protein. Such characteristic folding is particularly associated with proteins like
myoglobin and many of the enzymes—proteins that function as catalytic and carrier
molecules.Example – Myoglobin

Quaternary Structure

• Proteins are actually composed of two or more separable polypeptide chains. The
aggregation of multiple polypeptides to form a single functioning protein is called the
quaternary structure of a protein.
• Many of the enzymes that function in metabolism consist of as many as four to six
polypeptide subunits.
• Changes in the kinds or arrangements of these subunits lead to alternative forms of the
enzyme called isozymes.
• Example – Hemoglobin,DNA Polymerase

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PROTEIN FUNCTIONS:
Proteins are the basic constituents of cell cytoplasm.
Fundamental constituents of structure & functional organization of the cell.
Enzymes & hormones are proteins.
Proteins play a major part in the transport of oxygen & CO2 by haemoglobin.
Proteins like thrombin & fibrinogen participates in blood clotting as clotting factors.
Antibodies are protein in nature which acts as defense against infections.
Some proteins like actin & myosin carry out the mechanical work in the muscle.
Rhodopsin of retina carries out the function of sensing the light.
The plasma proteins functions in maintaining the homeostatic control of the volume of
circulating blood & interstitial fluids.
Examples :

Function Description Example

Immunogenic • Antibodies bind to specific foreign
particles, such as viruses and Immunoglobulin
bacteria, to help protect the body.
Cellular Metabolism - • DNA-associated
Enzymes proteins regulate chromosome struc
ture during cell division and/or play DNA polymerase,Ligase
a role in regulating gene
expression, for example, histones
and cohesin proteins

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 • Hormone proteins co-ordinate
Hormones bodily functions, example -
insulin controls our blood sugar Insulin,Dopamine
concentration by regulating the
uptake of glucose into cells.
.
• Contractile proteins are involved Actin,Myosin
Structural Component in muscle contraction and
movement
Transport • These proteins bind and carry Ferritin
atoms and small molecules
withincells and throughout the
body.
Digestive enzymes • Enzymes are proteins that Trypsin, pepsin
facilitate biochemical reactions, for
example, pepsin is
a digestive enzyme in
• your stomach that helps to break
down proteins in food.
Clinical Implications of Secondary Structure of Proteins
• The secondary structure of a protein can be altered by either a mutation in the primary sequence
of amino acids that make up the protein or by extreme conditions that force the proteins to
denature or lose their shape.
• Spongiform encephalopathy, and Amyloidosis are two classes of disease involving changes in the
secondary structure of proteins.
• Both involve the misfolding of proteins into Beta sheets, and the presence of these proteins
leading to tissue damage.

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