SIVAPRABHA T S

ASSISTANT PROFESSOR
DEPARTMENT OF BIOCHEMISTRY
SREE SANKARA COLLEGE, KALADY
The word “Proteins” comes from Greek word
“Proteios” meaning Primary/Holding the first
place/pre-eminent.

Out of the dry body weight 3/4th is made up of

proteins.
Proteins are made up of elements like – C, H,O & N
Some proteins also contains Sulphur and Phosphorous.

It also contains minor elements like

Fe, Cu, I, Mg, Mn, etc.

All proteins are polymers of Amino acids

Functions of proteins may be structural
and dynamic
Structural functions

(Other eg; are Elastin of connective tissue and

Dynamic functions Keratin of Hair and Nails)

Proteins which acts as enzymes and

polypeptide hormones direct and regulate
metabolism in the body

Blood Clotting factor like Fibrinogen which

is a plasma protein acts as first factor or
factor I
Immunoglobulins fight against infectious
diseases
⌛

Transport proteins Hemoglobin, Myoglobin and albumin

acts as transport proteins.

Storage proteins Hemosiderin , ferritin acts as

storage proteins.
(Fibrous Proteins)
 As the name indicates it consists of only one amino acid

(Fibrous Proteins)

Soluble in water and coagulated by heat. Eg., serum albumin, lactalbumin (Milk), Ovalbumin)

Soluble in dilute neutral salt solution. Eg (Egg Yolk & myosin of muscle)

Soluble in dilute acids and alkalies. Mostly found in cereals Eg., Oryzenin (rice), Glutelin (Wheat)

Insoluble in water, soluble in alcohol. Eg.,Zein (Corn) Glaidin (Wheat)

Histones are basic proteins. Eg.,Globin of Hb and Nucleohistone.

Soluble in water, not coagulated by heat and are strongly basic and hence
Protamines combine with acidic proteins. They occur in association with nucleic acids
Eg.,Nucleoprotein of Sperm.
 They are fiber like in shape and are not digestible. They are
(Fibrous Proteins) insoluble in water.

The most abundant protein in the body . It is the chief constituent

of connective tissue.

Elastin confers elasticity and extensibility to arteries and trendons.

It contains Desmosin and iso-desmosin cross linkages.

They are cysteine rich protein mostly seen in hair and nails.
 Proteins combined with a non-protein part
or prosthetic group

Proteins in combination with carbohydrates

(Fibrous Proteins)
Mucins, Plasma proteins

These are lipid complex with proteins

Act as transporter of Lipids

These are proteins attached to nucleic

acids Histone Proteins

These are proteins in combination with

coloured substances. Hb (Red), Flavoproteins
(Yellow) etc.

They contains metal ions as

prosthetic group. Ceruloplasmin (Cu),
Cytochrome (Iron), Carbonic
anhydrase (Zinc)
 These proteins do not occur in nature as such. They are
The degradative, denatured products of native proteins.

Formed by certain intramolecular

(Fibrous Proteins)
rearrangement of
protein structure.

When denatured (loss of native protein structure)

becomes irreversible, the protein is called
coagulum. When heated a protein is coagulated.

These are denatured proteins eg., Fibrin from

Fibrinogen.

They are formed by action of conc. Acids and

alkalies on proteins (eg., Acid metaproteins and
Alkalie metaproteins)
 These proteins do not occur in nature as such. They are
The degradative, denatured products of native proteins.

These are hydrolytic products

(Fibrous Proteins) of proteins and are smaller in size.

When denatured (loss of native protein structure)

becomes irreversible, the protein is called
ProteinsWhen heated
coagulum.
Proteans Metaproteins
a protein is coagulated.

These are denatured proteins eg., Fibrin from

Fibrinogen. Proteoses
Peptides Peptones Proteoses
They are formed by action of conc. Acids and
alkalies on proteins (eg., Acid metaproteins and
Alkalie metaproteins)
Amino acids
 If all the 10 essential amino acids are there
they are Complete proteins

If any one or two essential amino acids

is partially lacking it is partially
essential amino acid.

They completely lack one or two essential

amino acids, and cannot even maintain normal
. Zein from Corn body weight.
 Isoelectric pH is the pH at which it exists as
zwitter ion and carries no net charge making
At
the molecule electrically neutral.
I
S
O
E
L
E
C
T
R
I
C
PH
Conductivity and osmotic pressure are at minimum
This PI value indicates that it
exist in the cationic form below
that pH and exist in the anionic
form above that pH; and found
as zwitter ion at this pH.
 Buffer Action
Buffers are substances which resist change in body pH.

Amino acids with ionisable groups in

their side chain acts as buffers.

They act as buffers at their pk values.

For example : Histidine with Imidazole group (with a pH near 7).

Take part in homeostasis of blood pH.

Hb (contains Histidine in its core structure) acts as

intracellular buffer.
 Chemical Properties
Reactions involving –COOH group
1. Decarboxylation
Amino acids forms corresponding amines upon Decarboxylation.

Examples:

Ø Glutamate γ – amino butyric acid (GABA) + CO2

Neurotransmitter
Ø Histidine Histamine + CO2
Mediator of allergic reactions
Ø Tyrosine Tyramine + CO2
 2. Amide Formation
The –COOH group reacts with ammonia to form corresponding amide.

For Example:

Aspartic acid + NH3 Aspargine

Glutamic acid + NH3 Glutamine

Reaction involving amino ( -NH2) group
1. Transamination:

Transfer of amino group from one

amino acid to a keto acid forming a new amino
acid is known as transamination.

Importance:

Interconvertion of amino acids and

synthesis of non-essential amino acids occur
through transamination.
Reaction involving amino ( -NH2) group
2. Deamination:

The α- amino group is removed from

the amino acid to form corresponding keto
acid and ammonia.

Ammonia is released from Glutamic acid

undergoing oxidative deamination.
Reaction involving amino ( -NH2) group

3. Formation of Carbamino compounds:

CO2 combines with a amino group forming

carbamino compounds.

Importance:

This is the underlying mechanism of the

transport of CO2 from tissues to lungs by Hb.
Reaction involving Side Chain:

1. Reactions by -OH group

The hydroxyl group of Serine and Threonine are

involved in the formation of phosphoproteins.

Importance

Phosphorylation and dephosphorylation of

enzymes play a crucial role in the regulatory
mechanism of metabolic pathways.
Reaction involving Side Chain:

2.Reactions of –SH group

Sulfhydral groups of cysteine residues take part in

disulphide bonds forming Cystine.

3.Reactions by amide group

The amide groups of glutamine and aspargine form

N- Glycosidic linkages with carbohydrates forming
Glycoproteins.
It is a protein hormone
secreted by the β-cells of Mol.wt -5734
Islets of Langerhans

It consists of two poly peptide

chains A-chain and B-chain
Mol.wt -5734
3
 Lyophilisation (Freeze drying)
Lyophilisation is the process by which water is evaporated at
very low temperature in vaccum.

Eg: Formaldehyde will fix the three dimensional protein intact, and
afterwards other physical and chemical agents will not denature the
proteins .

This is the basis of fixation during

histopathological examinations