Session - 5 Introduction and Classification of Proteins

SESSION - 5
Introduction and Classification of Proteins

Introduction to Proteins
Among the macromolecules found in the living system proteins are the most abundant and are
diverse in their structure and function. . Each cell of the living organism contains thousands of
proteins each having its own unique function. Although proteins are diverse in their structure
and function, all proteins are made up of one or more chains of amino acids.
Types and functions of proteins
Proteins plays a very important role in cells or organisms and they function differently with
different functions and are they are very important in the living organisms including human
being. The following are various protein types with their various functions.
Proteins Function as Enzymes
Enzymes act as catalysts in biochemical reactions by increasing the speed of the reaction. The
enzymes are specific to its substrates to which it reacts. Different enzymes participate in
different types of reactions and they may breakdown, modify and rearrange break down, link
up, or rearrange their substrates.
Example: Salivary amylase breakdown starch into simple sugars.
Proteins Function as Hormones
Hormones are chemical signals which travel long distance in our body released by endocrine
cells (like the cells of your pituitary gland). The physiological processes in our body such as
growth, development, metabolism and reproduction are controlled by these hormones.
For example, insulin is an important peptide hormone that helps regulate blood glucose levels.
Spme other types of proteins and their functions are shown brlow
Role Examples Functions
As Digestive Breaking macro molecules in the food for
Amylase, lipase, pepsin
Enzyme easy absorption
As Transport Transport molecules ito different parts of
Hemoglobin
Molecule the body
As Structure Build different structures like cytoskeletion
Actin, tubulin, keratin
Molecule in the body
As Hormone Coordinate the activity of different body
Insulin, glucagon
signaling systems
As Defense
Antibodies Protect against foreign antigens
Mechanism
As Contraction Myosin Helps in contraction of muscles
As Storage
Legume storage proteins, egg Store food and energy for developmental
Molecule
white (albumin) processes.
Proteins have different size and shapes some are globular and some are fibrillary in shape. . For
example, the hemoglobin protein that carries oxygen in the blood is a globular protein, while
collagen, found in our skin, is a fibrous protein.
The shape of protein is very important in the function of the protein; many different types of
chemical bonds may be important in maintaining this shape. Changes in different environmental
factors such as temperature and pH, the presence of certain chemicals, may inactivate the
structure and function of protein and this process is usually called as denaturation.
Amino acids are the monomers that make up proteins. Proteins are made up of and each chain
is called as a polypeptide.
Peptide bonds
Every protein inside the cell contains polypeptide chains which are made of amino acids joined
together in a specific order. A polypeptide chain is long chain amino acid sequence. The
chemical properties and order of the amino acids are key in determining the structure and
function of the polypeptide. The amino acids of a polypeptide are attached to the next amino
acid by covalent bonds known as a peptide bonds. Each peptide bond is formed by the
dehydration reaction. The carboxyl group of the amino acid at the end of the polypeptide chain
reacts with the amino group of an incoming amino acid, releasing a molecule of water. The
resulting bond between amino acids is a peptide bond
Fig 1.: Formation of peptide bond between two amino acids

Image Source: https://cnx.org/contents/GFy_h8cu@9.85:2zzm1QG9@7/Proteins
The polypeptide chains of proteins have directionality due to the structure of the amino acids.
The two ends of the polypeptide chains are chemically distinct from one another. At one end,
the polypeptide has a free amino group, and is called the amino terminus also called as N-
terminus. The other end, which has a free carboxyl group, is known as the carboxyl
terminus also called as C-terminus. The N-terminus is on the left and the C-terminus is on the
right for the very short polypeptide shown above.
Classification of Proteins
Based on the structure, function, chemical nature, solubility and nutritional importance proteins
are classified into three main categories.
• Functional classification of proteins
• Chemical nature and solubility
• Nutritional importance
Continued in Session 6
References
• Smith, C. M., Marks, A. D., Lieberman, M. A., Marks, D. B., & Marks, D. B. (2005). Marks’
basic medical biochemistry: A clinical approach. Philadelphia: Lippincott Williams &
Wilkins. Smith, C. M., Marks, A. D., Lieberman, M. A., Marks, D. B., & Marks, D. B.
(2005). Marks’ basic medical biochemistry: A clinical approach. Philadelphia: Lippincott
Williams & Wilkins.
• Rodwell, V. W., Botham, K. M., Kennelly, P. J., Weil, P. A., & Bender, D. A. (2015). Harper’s
illustrated biochemistry (30th ed.). New York, N.Y.: McGraw-Hill Education LLC.
• John W. Pelley, Edward F. Goljan (2011). Biochemistry. Third edition. Philadelphia: USA.
• https://chemistry.tutorvista.com/biochemistry/proteins.html
• http://www.biologydiscussion.com/proteins/proteins-definition-importance-and-
classification-biochemistry/41903
• https://www.particlesciences.com/news/technical-briefs/2009/protein-structure.html
• http://www.biologydiscussion.com/proteins/proteins-functions-structure-properties-
and-classification/16912
SESSION - 6
Proteins are broadly classified based on their
• Solubility and composition
• Function
• Shape & size
A. Classification based on solubility and composition

Based on the solubility and composition protein are classified into three main groups as simple, conjugated
and derived proteins.
(i) Simple proteins
Simple proteins yield only amino acids after hydrolysis
Based on the solubility in different solvents simple proteins are further classified into as below:
Albumins
• Albumins are readily soluble in water, dilute acids and alkalies
• Albumins are coagulated by heat.
• Using high concentration of salt albumin can be precipitated out by the process of ‘Salting Out’
• They are deficient in glycine.
• Serum albumin and ovalbumin (egg white) are examples.
Globulins
• Globulins are insoluble in water but their solubility can be increased by the addition of salts such as
Sodium Chloride.
• Globulins are coagulated when exposed to high temperature
• They are deficient in methionine.
• Serum globulin, fibrinogen, myosin of muscle and globulins of pulses are examples.
Prolamins
• Prolamins are soluble in 70% alcohol and insoluble in water
• Prolaminws yield more proline and amide nitrogen on hydrolysis, hence the name prolamin.
• These proteins are lysin deficient
• Gliadin of wheat and zein of corn are examples of prolamins.
Glutelins
• Gluteins are insoluable in water and alcohol and s soluble in acids and alkalies
• Gluteins are usually plant proteins e.g., glutenin of wheat.
Histones
• Histones are small and stable basic proteins
• Histones usually contain large amount of Histidine amino acid.
• Histones are soluble in water and Insoluble in ammonium salts
• Histones are not readily coagulated when exposed to high temperature
• They are present in Nucleo Proteins.
Protamines
• Protamines are the simplest form of proteins. .
• They are soluble in water and not coagulate when heat to high temperature.
• They are basic proteins due to the presence of large quantities of arginine.
Albuminoids
• These proteins are highly stable and insoluble in water and salt solutions.
• These proteins are very similar to albumins and globulins.
• These proteins are highly resistant to proteolytic enzyme activity.
• They are fibrous in nature.
• They occur as chief constituent of exoskeleton structure such as hair, horn and nails.
ii. Conjugated or compound proteins

These are simple group of proteins combined with non-proteins substances called as Prosthetic Group.
The prosthetic group nature is the basis for the sub classification of conjugated proteins.
Nucleoproteins
• Nucleoproteins are simple basic proteins with histones in salt combination with nucleic acids as the
prosthetic group.
• They are the important constituents of nuclei and chromatin.
Mucoproteins
• These proteins are composed of simple proteins in combination with carbohydrates, which include
hyaluronic acid and chondroitin sulphates.
• Nucleoproteins are readily denatured by heat and easily precipitated by tri chloro acetic acid or picric
acid.
Chromoproteins
• These are proteins containing coloured prosthetic groups e.g., haemoglobin, flavoprotein and
cytochrome.
Lipoproteins
• These are proteins conjugated with lipids such as neutral fat, phospholipids and cholesterol
Metalloproteins
• Proteins binding to metal ions are called Metallo proteins.
• Ttransferrin a kind of metallo 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.
Phosphoproteins
• These proteins usually contains phosphoric acid hence the name.
• Phosphoric acid is linked to the hydroxyl group of certain amino acids like serine in the protein e.g.,
casein of milk.
iii. Derived proteins
These are the proteins derived from the partial or complete hydrolysis of simple and conjugated proteins by
the of the acids, alkalies and enzymes.
Derived proteins are classified into two types:
• Primary Derived Proteins
• Secondary Derived Proteins.
Primary-derived proteins
• These proteins are formed when the proteins undergo a single changes in their structure and
properties.
• The peptide bond in these proteins undergo non hydrolytic cleavage.
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.
Metaproteins
• These are formed by the action of acids and alkalies
• 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
• Secondary derived proteins are formed by the progressive hydrolytic cleavage of the peptide bonds
of the proteins.
• Based on their average molecular weight these proteins 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.
• These proteins are soluble in water and not coagulated when heated to high temperature.
• Peptides are containing very few amino acids.
References
Williams & Wilkins.
SESSION - 7
Proteins are broadly classified based on their
• Solubility and composition
• Function
• Shape & size
B. Classification of proteins based on function

Based on the function proteins are variously classified as below
1. Catalytic proteins – Enzymes

• One of the most important function of the proteins in the living system is to function as
Biocatalyst and these protein biocatalysts are called as Enzymes.
• Enzymes represent the largest class of proteins and nearly 2000 different kinds of
enzymes are known which carry out different kinds of reactions inside cells. Enzymes
increases the rate of the reaction.
2. Regulatory proteins - Hormones

• These are the polypeptides and small proteins found in the very low concentrations in
the animal kingdom, but plays a very important role in maintaining and regulating the
metabolic reactions.
e.g., growth hormone, insulin etc.
3. Protective proteins - Antibodies

• These proteins play a very important role in the defense mechanism of the body by
combining with the forge in antigens and fighting against the infectious diseases.
• The spleen and lymphatic system in the human body produces these protective proteins
in response to foreign antigens.
• The newly produced protein is called as Antibody which combines with the antigen and
fights against the disease progression.
4. Storage proteins
• These proteins are very important class of proteins which a very important role in
storage of amino acids and acts as the building blocks for the developing embryos.
• The storage proteins are responsible for storing essential amino acids which cannot be
synthesized by the human body.
• The major storage proteins in rice is Glutens, Albumin in egg and Casein in Milk.
5. Transport proteins
• These are the proteins responsible for transporting the special molecules throughout the
body in the blood.
• Hemoglobin is responsible for transporting the oxygen in the blood and Myoglobin us
responsible for transporting the oxygen in the muscles.
6. Structural proteins
• These proteins act as source of structural material which is the important component of
the extracellular fluids.
• Some of the structural proteins are Myosin of muscles, Keratin of skin, hair and nails,
Collagen of the connective tissue.
• Carbohydrates, fats, minerals and other cellular components are organized around such
structural proteins that form the molecular framework of living material.
7. Contractile proteins
• Action and Myosin are the important contractile proteins which plays the role in the
contractile system of the skeletal muscles.
8. Secretary proteins
• Fibroin is one of the secretory proteins produced by spiders and silkworm for building
their webs and cocoons.
C. Classification based on size and shape

Based on the size and shape proteins are classified into two types as;
• Globular Proteins
• Fibrous Proteins.
1. Globular proteins
• Globular proteins are soluble in water and fragile in nature enzymes, hormones,
antibodies are examples of globular proteins.
2. Fibrous proteins
• These proteins are tough and soluble in water and they used to build materials used to
support and protect specific tissues such as skin nails, keratin etc.,
References
Williams & Wilkins.
SESSION - 8
Levels of Protein Structure
The structure of the proteins is studied in four levels of organization
• Primary Structure
• Secondary Structure
• Tertiary Structure
• Quaternary Structure
1. Primary Structure of Protein

• The Primary structure of proteins is a linear sequence of amino acid chains in an exact order. .
• The linear sequence of the amino acids chains in the proteins is very important in determining the
three dimensional structure and function of the protein.
• Two or more polypeptides chains join together to form proteins and the amino acid sequence in
these polypeptide chains are very specific for each protein. Any changes in the amino acid sequence
will alter the structure and functions of the proteins.
The following is the primary structure of proteins with the linear sequence of amino acids within the
polypeptide chains which is important for the proper functioning of the proteins. This sequence is encoded in
the DNA genetic code. Any mutation in the DNA leads to changes in the amino acid sequence which finally
leads to changes in the protein structure and function.
Fig. 1: Primary Structure of Protein
Image Source:www.angelo.edu
The protein ‘s primary structure is the amino acid sequence in its polypeptide chain. Covalent, peptide bonds
which connect the amino acids together maintain the primary structure of a protein.
2. Secondary Structure of Protein
The secondary structure determines the overall configurational relationship between the linear
sequence of the amino acid residues. Secondary and tertiary levels of protein structure are
preserved by noncovalent forces or bonds like hydrogen bonds, electrostatic bonds,
hydrophobic interactions and van der Waals forces. In secondary structure the proteins are
formed by just joining of the simple polypeptide chains.
Secondary structure of proteins exists in two different types of structure α – helix and β –
pleated sheet structures.
Fig. 2: Secondary Structure of Protein
(a) α – Helix:
In 1951 Puling (Nobel prize, 1954) and Corey described the alpha helix and beta-pleated sheet structures
of polypeptide chains. The alpha helix is the most common and stable conformation for a polypeptide
chain. In proteins like hemoglobin and myoglobin, the alpha helix is abundant, whereas it is virtually
absent in chymotrypsin.
The alpha helix is a spiral structure (Fig. 2). The polypeptide bonds form the back-bone and the side
chains of amino acids extend outward. The structure is stabilized by hydrogen bonds between NH and
C=O groups of the main chain. Each turn is formed by 3.6 residues. The distance between each amino
acid residue (translation) is 1.5 Å. The alpha helix is generally right handed. Left handed alpha helix is
rare, because amino acids found in proteins are of L-variety, which exclude left handedness.
(b) β – pleated sheet:
The polypeptide chains in beta-pleated sheet is almost fully extended. The distance between
adjacent amino acids is 3.5Å. It is stabilized by hydrogen bonds between NH and C=O groups of
neighboring polypeptide segments. Adjacent strands in a sheet can run in the same direction
with regard to the amino and carboxy terminal ends of the polypeptide chain (parallel) or in
opposite direction (anti-parallel beta sheet) (Fig. 2). Betapleated sheet is the major structural
motif in proteins like silk Fibroin (anti-parallel), Flavodoxin (parallel) and Carbonic anhydrase
(both). Beta bends may be formed in many proteins by the abrupt U-turn folding of the chain.
Intrachain disulfide bridges stabilize these ben3.
Interactions of Protein Folding in Tertiary and Quaternary Structure
• Hydrophobic Interactions
Result from the attraction of nonpolar groups, or when they are forced together by their
mutual repulsion of the aqueous solvent. These interactions are particularly important
between the benzene rings in phenylalanine or tryptophan. This type of interaction is
relatively weak, but since it acts over large surface areas, the net effect is a strong
interaction.
• Hydrogen Bonding
Can form between a variety of side chains, especially those that contain: -OH -NH2- C-
NH2-
Hydrogen bonding also influences the secondary structure, but here the hydrogen
bonding is between R groups, while in secondary structures it is between the C=O and
NH portions of the backbone
• Salt Bridges
Are attractions between ions that result from the interactions of the ionized side chains
of acidic amino acids (—COO- ) and the side chains of basic amino acids (—NH3 + ).
• Disulfide Bridges
Can form between two cysteine residues that are close to each other in the same chain,
or between cysteine residues in different chains. These bridges hold the protein chain in
a loop or some other 3D shape
• Dipole-Dipole and Ion-Dipole Forces
Dipole-dipole attractive forces can occur between polar side-chains and/or peptide
groups.
References
Williams & Wilkins.
• https://www.angelo.edu/faculty/kboudrea/index_2353/Chapter_09_2SPP.pdf
SESSION - 9
3. Tertiary Structure of Protein
Secondary structure denotes the configurational relationship between residues which are about
3–4 amino acids apart; or secondary level defines the organization at immediate vicinity of
amino acids. The tertiary structure denotes three dimensional structure of the whole protein
(Fig .3). The tertiary structure defines the steric relationship of amino acids which are far apart
from each other in the linear sequence, but are close in the three-dimensional aspect. The
tertiary structure is maintained by noncovalent interactions such as hydrophobic bonds,
electrostatic bonds and van der Waals forces. The tertiary structure acquired by native protein is
always thermodynamically most stable.
Fig. 3: Tertiary Structure of Protein
4. Quaternary Structure of Protein

The spatial arrangement of various tertiary structures gives rise to the quaternary structure.
Some of the proteins are composed of two or more polypeptide chains referred to as sub-units.
The spatial arrangement of these subunits with respect to each other is known as quaternary
structure.
Fig. 4: Quaternary Structure of Protein
The exact amino acid sequence of each protein drives it to fold into its own unique and
biologically active three-dimensional fold also known as the tertiary structure. Proteins consist
of different combinations of secondary elements some of which are simple whereas others are
more complex. Parts of the protein chain, which have their own three-dimensional fold and can
be attributed to some function are called “domains”. These are considered today as the
evolutionary and functional building blocks of proteins.
Many proteins most of which are enzymes contain organic or elemental components needed for
their activity and stability. Thus the study of protein evolution not only gives structural insight
but also connects proteins of quite different parts of the metabolism.
Rules of Protein Structure
• The type determines the function of a protein.

• A protein’s shape is determined by its primary structure (the amino acid sequence).
• The amino acid sequence within a protein is determined by the encoding sequence of
nucleotides in the gene (DNA).
Summary of Protein Structure

Linderstrom-Lang (1952) in particular first suggested a hierarchy of protein structure with four
levels: central, secondary, tertiary, and quaternary. You are already familiar with this hierarchy,
because the most useful starting point for teaching basic protein structure is this structural
grouping.
• The primary structure of protein is the hierarchy’s basic level, and is the particular linear
sequence of amino acids comprising one polypeptide chain.
• Secondary structure is the next level up from the primary structure, and is the regular
folding of regions into specific structural patterns within one polypeptide chain.
Hydrogen bonds between the carbonyl oxygen and the peptide bond amide hydrogen
are normally held together by secondary structures.
• Tertiary structure is the next level up from the secondary structure, and is the particular
three-dimensional arrangement of all the amino acids in a single polypeptide chain. This
structure is usually conformational, native, and active, and is held together by multiple
noncovalent interactions.
• Quaternary structure is the next ‘step up’ between two or more polypeptide chains
from the tertiary structure and is the specific spatial arrangement and interactions
References
Williams & Wilkins.
SESSION - 10
Properties of Proteins
Physical Properties of Proteins
Solubility in Water
• The Protein-Water relationship is very complex. The interaction of peptide bonds in the
secondary structure of proteins is with water through hydrogen bonding.
• Hydrogen bonds with water is also formed between the alpha and beta helix structures
of the proteins.
• At the tertiary structure, water causes the orientation of the chains and hydrophilic
radicals to the outside of the molecule, while the hydrophobic chains and radicals tend
to react with each other within the molecule (hydrophobic effect).
Denaturation and Renaturation

• Physical and chemical agents can denature the proteins by unfolding the polypeptide
chains and causing hydrolysis of the peptide bonds.
• Denaturing agents denature the secondary and tertiary structure without affecting the
primary structure.
• If the denaturing agents are removed and the proteins returns back to its native state
and this process is called as Renaturation.
• Some of the denaturing agents include
Physical agents: Heat, radiation, pH
Chemical agents: Urea solution which forms new hydrogen bonds in the protein, organic
solvents, detergents.
Coagulation
• Coagulation is the aggregates of the proteins when denatured to high temperature and
all proteins will not coagulate at high temperatures, proteins like albumins, globulins will
coagulate at high heat.
Isoelectric point
• The point at which the number of positive charges and the number of negative are in
equilibrium and the net charges on the amino acids is zero is called as Isoelectric Point
(Pi).
• When electric field is applied to proteins at isoelectric point, the proteins do not move
towards anode or cathode and this properties of proteins is used to isolate the unique
proteins.
Molecular Weights of Proteins

• In general, the average weight of the amino acid in the polypeptide chain of the protein
is 110 and the molecular weight of the overall protein is calculated by total number of
amino acids multiplied by 110.
• Since different proteins have different amino acids sequence the molecular weight of
different proteins will be different. The molecular weights of proteins range from 5000 to
109 Daltons.
Posttranslational modifications
• After the proteins are synthesized on the ribosomes undergo various metabolic
processes such as psphorylation, glycosylation, ADP ribosylation, methylation,
hydroxylation, and acetylation affect the charge and the interactions between amino
acid residues, altering the three-dimensional configuration and, thus, the function of the
protein
Chemical Properties of Proteins

• Hydrolysis
Proteins are hydrolyzed by a variety of hydrolytic agents.
A. By acidic agents: Proteins, upon hydrolysis with conc. HCl (6–12N) at 100–110°C for 6
to 20 hrs, yield amino acids in the form of their hydrochlorides.
B. By alkaline agents: Proteins may also be hydrolyzed with 2N NaOH.
• Reactions involving COOH Group
A. Reaction with alkalies (Salt formation)
B. Reaction with alcohols (Esterification)
C. Reaction with amines
• Reactions involving NH2 Group
• Reaction with mineral acids (Salt formation): When either free amino acids or
proteins are treated with mineral acids like HCl, the acid salts are formed.
• Reaction with formaldehyde: With formaldehyde, the hydroxy-methyl derivatives
are formed.
• Reaction with benzaldehyde: Schiff ‘s bases are formed
• Reaction with nitrous acid (Van Slyke reaction): The amino acids react with HNO2
to liberate N2 gas and to produce the corresponding α-hydroxy acids.
• Reaction with acylating agents (Acylation)
• Reaction with FDNB or Sanger’s reagent
• Reaction with dansyl chloride
• Reactions involving both COOH AND NH2 Group
• Raction with triketohydrindene hydrate (Ninhydrin reaction)
• Reaction with phenyl isocyanate: With phenyl isocyanate, hydantoic acid is
formed which in turn can be converted to hydantoin.
• Reaction with phenyl isothiocyanate or Edman reagent
• Reaction with phosgene: With phosgene, N-carboxyanhydride is formed
Reaction with carbon disulfide: With carbon disulfide, 2-thio-5-thiozolidone is
produced
• Reactions involving R Group or Side Chain
A. Biuret test
B. Xanthoproteic test
C. Millon’s test
D. Folin’s test
E. Sakaguchi test
F. Pauly test
G. Ehrlich test
• Reactions involving SH Group
• Nitroprusside test: Red colour develops with sodium nitroprusside in dilute
NH4.OH. The test is specific for cysteine.
• Sullivan test: Cysteine develops red colour in the presence of sodium 1, 2-
naphthoquinone- 4-sulfonate and sodium hydrosulfite.
References
Williams & Wilkins.
Lecture 12
Proteins
Classification of protein
Proteins are classified based on their
 Solubility and composition
 Function
 Shape & size
A. Classification based on solubility and composition
According to this classification, proteins are divided into three main groups as
simple, conjugated and derived proteins.
(i) 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.
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.
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.
ii. 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.
Mucoproteins
 These proteins are composed of simple proteins in combination with
carbohydrates like mucopolysaccharides, which include hyaluronic acid and
chondroitin 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 small
amounts of carbohydrate usually less than 4% hexosamine.
Chromoproteins
 These are proteins containing coloured prosthetic groups e.g., haemoglobin,
flavoprotein and cytochrome.
Lipoproteins
 These are proteins conjugated with lipids such as neutral fat, phospholipids
and cholesterol
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.
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.
iii. 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 and
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.
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.
 The complete hydrolytic decomposition of the natural protein molecule into amino
acids generally progresses through successive stages as follows:
Protein -----> Protean ------- Metaprotein
Proteoses ------>Peptones ------->Peptides ------ amino acids
b. 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.
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.
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.
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.
C. Classification based on size and shape
Based on size and shape, the proteins are also subdivided into globular and
fibrous proteins.
 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
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Session - 5 Introduction and Classification of Proteins

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Session - 5 Introduction and Classification of Proteins

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SESSION - 5

Introduction and Classification of Proteins

Fig 1.: Formation of peptide bond between two amino acids

A. Classification based on solubility and composition

ii. Conjugated or compound proteins

B. Classification of proteins based on function

1. Catalytic proteins – Enzymes

2. Regulatory proteins - Hormones

3. Protective proteins - Antibodies

C. Classification based on size and shape

Levels of Protein Structure

The structure of the proteins is studied in four levels of organization

1. Primary Structure of Protein

Fig. 1: Primary Structure of Protein

2. Secondary Structure of Protein

Fig. 2: Secondary Structure of Protein

(b) β – pleated sheet:

Levels of Protein Structure

Fig. 3: Tertiary Structure of Protein

4. Quaternary Structure of Protein

Fig. 4: Quaternary Structure of Protein

Rules of Protein Structure

• The type determines the function of a protein.

Summary of Protein Structure

Denaturation and Renaturation

Molecular Weights of Proteins

Chemical Properties of Proteins

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