Introduction of proteins

The word “protein” Originates from the Greek word “proteios” which means of prime
importance or holding first place.
Importance of proteins
 Proteins are crucial for enzymatic activity, structural support, and transport in the
body.
 Play a vital role in immune response and cell signaling.
 Can be catabolize to supply energy
 Several hormones are proteins in nature.
 Some proteins present in cell membrane, cytoplasm and nucleus of the cell act as
receptors.
 Storage proteins bind with specific substance and store them, e.g. Iron is stored as ferritin
Composition of proteins
 In addition to C, H, and O which are present in carbohydrates and lipids, proteins also
contain N which is about16% of its weight.
 Amino acids are the building blocks of proteins (which are large molecules with high
molecular weight about 5000 to 25,000,000).
 They are organic compounds containing amino group (-NH2) and a carboxylic
group (COOH).
 Proteins are the unbranched polymers of L-a-aminoacids.
General formula

 Where R is side chain (H, Aliphatic, aromatic, etc.)

 Side chain varies from one amino acid to other.

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 Classification of Amino acids:
Amino acids are classified into 3 groups depending on their reaction in solution
A. Neutral Amino Acids
B. Acidic Amino Acids
C. Basic Amino Acids

A. Neutral amino acids:

This is the largest group of amino acids. Sub divided into,
a) Aliphatic
b) Aromatic
c) Heterocyclic
d) Imino acids
e) “S” containing Amino acids
a) Aliphatic Amino acids:
1. Glycine
2. Alanine
3. Valine
4. Leucine
5. Isolucine
b) Aromatic amino acids:
Second group of neutral amino acids consists of aromatic amino acids
1. Phenylalanine
2. Histidine
3. Tyrosine
4. Trytophan
c) Heterocyclic amino acids:
1. Tryptophan
This amino acid is often considered as aromatic since it has aromatic ring in its structure
d) Imino Acids:
1. proline
e) “S” containing Amino acids:
1. Cysteine
2. Methionine

B. Acidic amino acids: These amino acids have 2–COOH groups and 1 – NH group. They are
there for mono amino di carboxylic acids.
1. Aspartic acid
2. Glutamine
3. Asparagine
4. Glutamic Acid

C. Basic amino acids: This class of amino acids consists of those amino acids which have
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 1–COOH group and 2–NH2 groups. Thus they are diamino monocarboxylic acids.
1. Arginine
2. Lysine
3. Histidine

Essential Amino Acids

Nutritionally, amino acids are of two types:
(a) Essential
(b) Non-essential.
(c) There is also a third group of semi-essential amino acids.
(a) Essential amino acids:
Which are not synthesized by the body and must be taken in the diet.
They include
 valine,
 leucine,
 isoleucine,
 phenylalanine,
 threonine,
 tryptophan
 Arginine
 Methionine
 Histidine
(b) Non-essential amino acids: They can be synthesized by the body.
(c) Semi-essential amino acids: These are growth promoting factors. They are not
synthesized in sufficient quantity during growth. They include
 arginine
 histidine.

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 Classification of Proteins

Proteins are classified:

I. On the basis of shape and size
II. On the basis of functional properties
III. On the basis of solubility and physical properties.

I. On the basis of shape and size

• Fibrous Proteins: When the axial ratio of length:width of a protein molecule is
more than10, it is called a Fibrous protein.
Examples: α-keratin from hair, collagen.
• Globular protein: When the axial ratio of length: width of a protein molecule is
less than10, it is called as Globular protein.
Examples: Myoglobin, haemoglobin, ribonuclease etc.

II. On the basis of functional properties:

• Defense proteins: Immunoglobulins involved in Defence mechanisms.
• Contractile proteins: Proteins of skeletal muscle Involved in muscle contraction
and relaxation.
• Respiratory proteins: Involved in the function of Respiration, like haemoglobin,
myoglobin, cyto-Chromes.
• Structural proteins: Proteins of skin, cartilage, nail.
• Enzymes: Proteins acting as enzymes.
• Hormones: Proteins acting as hormones.

III. On the basis of solubility and physical properties

On the basis of solubility and physical properties proteins are divided into three classes:
A. Simple protein:
These are protein which on complete hydrolysis yield only amino acids.
 These are further sub classified on the basis of their solubility and physical properties
and heat coagulation abilities:
• Protamines: Small molecules are soluble in water, dilute acid and alkalies and non
Coagulable by heat. Rich in arginine and PH is around7.4.
Examples: salmine, sardinine and cyprine of fish and testes.
• Histones: basic proteins, rich in arginine and histidine, with alkaline isoelectric pH. They
do not readily coagulate on heating.
Examples: Nucleohistones, chromosomal nucleoproteinsAndglobinofhaemoglobin.
• Albumins: proteins which are soluble in water and in dilute salt solutions changed to
products that are insoluble in water and solutions of salt and Coagulable of heat.
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 Examples: Plant albumins: Legumelin in legumes, leuco-sinincereal.
• Glubulin: Globulins are insoluble in water but soluble in dilute Neutral salt solutions.
They are also heat coagulable. Examples:
Ovo globulinin eggs,
Lactoglobulin in milk, legumin from legumes.
• Gliadins:Alcohol soluble plant proteins, insoluble inwater or salt solutions and
absolute alcohol. Examples: Gliadin of wheat and horde in of barle
• Glutelins: These are plant proteins, insoluble in water or neutral Salt solutions, but
soluble in dilute acids or alkali
Examples:Oryzenin of rice and glutelin of wheat.
• Scleroproteins or Albuminoids: Scleroproteins or Albuminoids These are fibrous
proteins with great stability and very low solubility and form supporting structures of
animals. In this group are found keratins, collagens and elastins.

B. Conjugated proteins:
These are proteins which in addition to amino acids contain non protien group (prosthetic
group) in their structure. Sub classification
These are further sub classified into following:
a) Nucleoproteins The nucleoproteins are compounds made up of simple basic proteins such as
protamine or histone with Nucleic Acids as the prosthetic group.
b) Deoxyribonucleo proteins:: It contain DNA as prosthetic Group, are found in nuclei
mitochondria and chloro-Plasts.
c) Ribonucleoproteins: It occurs in nucleoli and ribosome Granules. They have RNA as
prosthetic group.
i. Examples: Nucleo histone and neucleo protamine.
d) Glycoproteins: Glycoproteins are the proteins with carbohydrate moiety as the prosthetic group.
Glycoproteins include mucins.
e) Chromoproteins: These are the proteins with phosphoric acid as organic Phosphate but not the
phosphate containing substances
f) Lipoproteins: The lipoproteins are formed in combination with lipids as their prosthetic group.
As the name indicates, they contain a metal ion as their prosthetic group.

C. Derived Protiens
These are protiens formed by native protein by the action of heat, physical for cesor
chemical factors
 Sub-classificaton:
 Primary Derived proteins
 Secondary Derived proteins
 Denatured or coagulated

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 General Properties of Proteins
1. Taste: Tasteless.(protein derived) are bitter in taste.
2. Odour: Odorless on heating turn brown and give odor of burning feather.
3. Molecular weight: Large molecular weight thus are macro molecules e.g. Serum albumin
(6900), Hemoglobin(67000)
4. Viscosity: Viscosity is closely related to molecular shape.long molecules more viscous than
globular proteins.
5. Hydration: Polar groups of proteins hydrated in presence of water.
when electrolytes, alcohol or sugar added they dehydrate protein and precipitate it from
solution.
6. Heat coagulation of protein: During coagulation protein denatured.
Coagulation is maximum at isoelectric pH of protein.
7. Amphoteric nature: Proteins have amino acids which on ionization produce anion and
cation. Depending upon pH acts as proton donor or proton acceptor,
Thus protein act both as an acid or base.
.At iso-electric pH protein exist as zwitter ion, equal numbers of positive and negative charges.
So at isoelectric pH charge on protein is zero.
8. Precipitation of Protein: Proteins can be precipitated by a number of +ve and-ve ions.
By +ve ions: Such as Zn+², Ca+2, Fe+3 (heavy metals) precipitate protein at pH
alkaline to its isoelectric pH.
By -ve ions: Negative ions combine with proteins at pH Acidic to its isoelectric pH.
-NH2 group is the reacting group in this case.
9. Colour reaction: Protein produce colour in certain reactions e.g.
 Millions test: give white ppt (tyrosine of protein)
 Sakaguchi test: give red color ppt (arginine of protein)
 Sullivan reaction: give reddish colour.

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 Properties of Amino Acids:

Physical Properties
1. Amino acids are colorless, crystalline solids.
2. All amino acids have a high melting point greater than 200o
3. Solubility: They are soluble in water, slightly soluble in alcohol, and dissolve with
difficulty in methanol, ethanol, and propanol. R-group of amino acids and pH of
the solvent play important role in solubility.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond involving
their amino and carboxylate groups. A covalent bond formed between the alpha-
amino group of one amino acid an danalpha-carboxylgroup of other forming -CO-
NH-linkage. Peptide bonds are planar and partially ionic.

Chemical Properties

Zwitter ionic property:

A zwitter ion is a molecule with functional groups, of which at least one has a positive and
one has a negative electrical charge. The net charge of the entire molecule is zero. Amino acids
are the best-known examples of zwitterions. They contain an amine group (basic) and a
carboxylic group (acidic). The -NH2 group is the stronger base, and so it picks up H+ from the -
COOH group to leave a zwitter ion. The (neutral) zwitter ion is the usual form of amino acids
that exist in the solution.

1. Amphoteric property:
Amino acids are amphoteric in nature that is they act as both acids and base due to the two
amine and carboxylic groups present.
2. Ninhydrintest:
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and heated, the
formation of a violet color indicates the presence of α-amino acids.
3. Reaction with Sanger’s reagent:
Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts with a free amino group in the peptide
chain in a mild alkaline medium under cold conditions.

4. Reaction with nitrous acid:

Nitrous acid reacts with the amino group to liberate nitrogen and form the
corresponding hydroxyl.

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 5. Peptide linkage
A peptide linkage is a chemical bond formed between two molecules when the carboxyl group of
one molecule reacts with the amino group of the other molecule, releasing a molecule of water
(H2O). for exampe
Valine and alanine can form the dipeptide valyalanine through the formation of a peptide
bond.
Example:

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