Classification

Proteins
 Protein

• Any of a class of nitrogenous organic

• A) Solubility and composition

• Simple protein
• Conjugated protein
• Derived proteins.
 1) Simple proteins
• Simple proteins yield on hydrolysis, only amino acids.
• These proteins are further classified based on their
solubility in different solvents as well as their heat
coagulability.
Albumins:
• Albumins are readily soluble in water, dilute acids and
alkalies
• Coagulated by heat.
• Seed proteins contain albumin in lesser quantities.
• Albumins may be precipitated out from solution using high
salt concentration, a process called 'salting out'.
• They are deficient in glycine.
• Serum albumin and ovalbumin (egg white) are examples.
 1) Simple proteins
Globulins
• Globulins are insoluble or sparingly soluble in
water, but their solubility is greatly increased by
the addition of neutral salts such as sodium
chloride.
• These proteins are coagulated by heat.
• They are deficient in methionine.
• Serum globulin, fibrinogen, myosin of muscle
and globulins of pulses are examples.
 1) Simple proteins
Prolamins
• Prolamins are insoluble in water but soluble in
70-80% aqueous alcohol.
• Upon hydrolysis they yield much proline and
amide nitrogen, hence the name prolamin.
• They are deficient in lysine.
• Gliadin of wheat and zein of corn are
examples of prolamins.
Glutelins
• Glutelins are insoluble in water and absolute
alcohol but soluble in dilute alkalies and acids.
• They are plant proteins e.g., glutenin of
wheat.
Histones
• Histones are small and stable basic proteins
• They contain fairly large amounts of basic
amino acid, histidine.
• They are soluble in water, but insoluble in
ammonium hydroxide.
• They are not readily coagulated by heat.
• They occur in globin of hemoglobin and
nucleoproteins.
 Protamines
• Protamines are the simplest of the proteins.
• They are soluble in water and are not
coagulated by heat.
• They are basic in nature due to the presence
of large quantities of arginine.
• Protamines are found in association with
nucleic acid in the sperm cells of
• certain fish.
• Tyrosine and tryptophan are usually absent in
protamines.
 Albuminoids
• These are characterized by great stability and
insolubility in water and salt solutions.
• These are called albuminoids because they are
essentially similar to albumin and globulins.
• They are highly resistant to proteolytic
enzymes.
• They are fibrous in nature and form most of
the supporting structures of animals.
• They occur as chief constituent of exoskeleton
structure such as hair, horn and nails.
 2) Conjugated or compound proteins
• These are simple proteins combined with
some non-protein substances known as
prosthetic groups.
• The nature of the non-protein or prosthetic
groups is the basis for the sub classification of
conjugated proteins.
Nucleoproteins
• Nucleoproteins are simple basic proteins
(protamines or histones) in salt combination
with nucleic acids as the prosthetic group.
• They are the important constituents of nuclei
and chromatin.
 2) Conjugated or compound proteins
Mucoproteins
• These proteins are composed of simple proteins in
combination with carbohydrates like
mucopolysaccharides, which include hyaluronic acid
andchondroitin sulphates.
• On hydrolysis, mucopolysaccharides yield more
than 4% of amino-sugars, hexosamine and uronic
acid e.g., ovomucoid from egg white.
• Soluble mucoproteins are neither readily denatured
by heat nor easily precipitated by common protein
precipitants like trichloroacetic acid or picric acid.
• The term glycoproteins is restricted to those
proteins that contain smal amounts of carbohydrate
usually less than 4% hexosamine.
2) Conjugated or compound proteins
Chromoproteins
• These are proteins containing coloured
prosthetic groups e.g., haemoglobin,
flavoprotein and cytochrome.
Metalloproteins
• These are metal-binding proteins.
• A -globulin, termed transferrin is capable of
combining with iron, copper and zinc.
• This protein constitutes 3% of the total plasma
protein.
• Another example is ceruloplasmin, which
contains copper.
2) Conjugated or compound proteins

Lipoproteins
• These are proteins conjugated with lipids such
as neutral fat, phospholipids and cholesterol.
Phosphoproteins
• These are proteins containing phosphoric acid.
• Phosphoric acid is linked to the hydroxyl group
of certain amino acids like serine in the
protein e.g., casein of milk.
 3) Derived proteins
• These are proteins derived by partial to
complete hydrolysis from the simple or
conjugated proteins by the action of acids,
alkalies or enzymes.
• They include two types of derivatives:
• primary-derived proteins
• secondary-derived proteins
 Primary-derived proteins
• These protein derivatives are formed by
processes causing only slight changes in the
protein molecule and its properties.
• There is little or no hydrolytic cleavage of
peptide bonds.
Proteans
• Proteans are insoluble products formed by the
action of water, dilute acids and enzymes.
• These are particularly formed from globulins
but are insoluble in dilute salt solutions.
• e.g., myosan from myosin, fibrin from
fibrinogen.
 Primary-derived proteins
Metaproteins
• These are formed by the action of acids and
alkalies upon protein.
• They are insoluble in neutral solvents.
Coagulated proteins
• Coagulated proteins are insoluble products
formed by the action of heat or alcohol on
natural proteins.
• e.g., cooked meat and cooked albumin.
 Secondary-derived proteins
• These proteins are formed in the progressive hydrolytic
cleavage of the peptide bonds of protein molecule.
• They are roughly grouped into proteoses, peptones
and peptides according to average molecular weight.
• Proteoses are hydrolytic products of proteins, which
are soluble in water and are not coagulated by heat.
• Peptones are hydrolytic products, which have simpler
structure than proteoses.
• They are soluble in water and are not coagulated by
heat.
• Peptides are composed of relatively few amino acids.
• They are water-soluble and not coagulated by heat.
 B)Classification based on size and
shape
• Based on size and shape, the proteins are also
subdivided into:
• Globular proteins are mostly water-soluble
and fragile in nature e.g., enzymes, hormones
and antibodies.
• Fibrous proteins are tough and water-
insoluble.
• They are used to build a variety of materials
that support and protect specific tissues, e.g.,
skin, hair, fingernails and keratin.
C) Classification of proteins based on
function
• Proteins are classified based on their functions
as:
Catalytic proteins – Enzymes
• The most striking characteristic feature of these
proteins is their ability to function within the
living cells as biocatalysts.
• These biocatalysts are called as enzymes.
• Enzymes represent the largest class.
• Nearly 2000 different kinds of enzymes are
known, each catalyzing a different kind of
reaction.
• They enhance the reaction rates a million fold.
 Protective proteins - Antibodies
• These proteins have protective defense function.
• These proteins combine with foreign protein and
other substances and fight against certain
diseases.
• e.g., immunoglobulin.
• These proteins are produced in the spleen and
lymphatic cells in response to foreign substances
called antigen.
• The newly formed protein is called antibody
which specifically combines with the antigen
which triggered its synthesis thereby prevents the
development of diseases.
• Fibrin present in the blood is also a protective
protein.
 Storage proteins
• It is a major class of proteins which has the
function of storing amino acids as nutrients and
as building blocks for the growing embryo.
• Storage proteins are source of essential amino
acids, which cannot be synthesized by human
beings.
• The major storage protein in pulses is globulins
and prolamins in cereals.
• In rice the major storage protein is glutelins.
• Albumin of egg and casein of milk are also
storage proteins.
 Transport proteins
• Some proteins are capable of binding and
transporting specific types of molecules through
blood.
• Haemoglobin is a conjugated protein composed
of colourless basic protein, the globin and
ferroprotoporphyrin or haem.
• It has the capacity to bind with oxygen and
transport through blood to various tissues.
• Myoglobin, a related protein, transports oxygen
in muscle.
• Lipids bind to serum proteins like albumin and
transported as lipoproteins in the blood.
 Toxic proteins
• Some of the proteins are toxic in nature.
• Ricin present in castor bean is extremely toxic
to higher animals in very small amounts.
• Enzyme inhibitors such as trypsin inhibitor
bind to digestive enzyme and prevent the
availability of the protein.
• Lectin, a toxic protein present in legumes,
agglutinates red blood cells.
• A bacterial toxin causes cholera, which is a
protein.
• Snake venom is protein in nature.
 Structural proteins
• These proteins serve as structural materials or
as important components of extra cellular
fluid.
• Examples of structural proteins are myosin of
muscles, keratin of skin and hair and collagen
of connective tissue.
• Carbohydrates, fats, minerals and other
cellular components are organized around
such structural proteins that form the
molecular framework of living material.
 Regulatory proteins - Hormones
• These are polypeptides and small proteins
found in relatively lower concentrations in
animal kingdom but play highly important
regulatory role in maintaining order in
complex metabolic reactions.
• e.g., growth hormone, insulin etc.
Contractile proteins
• Proteins like actin and myosin function as
essential elements in contractile system of
skeletal muscle.
 Secretary proteins
• Fibroin is a protein secreted by spiders and
silkworms to form webs and cocoons.

Exotic proteins
• Antarctic fishes live in -1.9oC waters, well
below the temperature at which their blood is
expected to freeze.
• These fishes are prevented from freezing by
antifreeze glycoproteins present in their body.
THE END