Chapter 4

Proteins Structure, Types and

Functions

Dr. M. CHANDRAN, M.Tech., Ph.D.,

Associate professor.,
Dept of Biotechnology.,
College of Biological and Chemical Engg.,
Mail ID: biochandran1976@gmail.com,
Cell Number :+251 0902642293
WhatsApp number: +91 9894093495
• Proteins are large, complex molecules that play many critical roles
in the body.
• They do most of the work in cells and are required
for the structure, function, and regulation of the body's tissues and
organs.
• There are 20 different types of amino acids that can be combined
to make a protein.
• Proteins account for 50% of the dry weight of the human body.
• Current recommended daily intake for adults is 0.8 grams of
protein per kg of body weight (more is needed for children).
• Dietary protein comes from eating meat and milk.
• 100,000 different proteins in human body
Peptide bond

A dipeptide forms:

• When an amide links two amino acids (Peptide bond).

• Between the COO− of one amino acid and

the NH3 + of the next amino acid.

peptide
bond
CH3 + O CH3 H O
+ O- H3N + N
H3N + O- H3N O - + H2 O
O CH2 OH O CH2 OH
Alanine (Ala) Serine (Ser) Alanylserine
(Ala-Ser)
 Structure of proteins
Protein structure is the three-dimensional arrangement of
atoms in an amino acid-chain molecule. Proteins are polymers
– specifically polypeptides – formed from sequences of amino
acids, the monomers of the polymer. Protein structures range
in size from tens to several thousand amino acids.

1. Primary structure

2. Secondary structure

3. Tertiary structure

4. Quaternary structure
 Primary =
sequence of aa’s
 Secondary =
forms pleated
sheet, helix, or
coil
 Tertiary = entire
length of aa’s
folded into a
shape
 Quaternary =
several aa
sequences linked
together
 Primary Structure of proteins

- The order of amino acids held together by peptide bonds.

- Each protein in our body has a unique sequence of amino acids.
- The backbone of a protein.
- All bond angles are 120o, giving the protein a zigzag arrangement.

CH3
CH3 S
CH CH3 SH CH2
+
CH3 O
+ CH O CH2 O CH2 O
H3N CH C N CH C N CH C N CH C O-
H H H

Ala─Leu─Cys─Met
 Disulfide Bond

The -SH (sulfhydryl) group of cysteine is easily oxidized

to an -S-S- (disulfide).

+ -
H3 N-CH-COO
CH2 a disulfide
+ oxidation bond
2 H3 N-CH-COO- S
CH2 reduction S
SH + CH2 -
Cysteine H3 N-CH-COO
Cystine
 NH3+ NH3+
Example of Primary Structure of proteins

The primary structure of insulin:

- Is a hormone that regulates the glucose level in the
blood.

- Was the first amino acid order determined.

- Contains of two polypeptide chains linked by

disulfide bonds (formed by side chains (R)).

- Chain A has 21 amino acids and O C

O-
chain B has 30 amino acids.

- Genetic engineers can produce it for treatment of

diabetes.
O C
O-
Chain A Chain B
 Secondary Structure of proteins

Describes the way the amino acids next to or near to each other
along the polypeptide are arranged in space.

1. Alpha helix (α helix)

2. Beta-pleated sheet (-pleated sheet)

3. Triple helix (found in Collagen)

4. Some regions are random arrangements.

 Secondary Structure - α-helix

• A section of polypeptide chain coils into a

rigid spiral.

• Held by H bonds between the H of N-H

group and the O of C=O of the fourth amino
acid down the chain (next turn).

• looks like a coiled “telephone cord.”

• All R- groups point outward from the helix.

H-bond

• Myosin in muscle and α-Keratin in hair

have this arrangement.
 Secondary Structure - -pleated sheet
• Consists of polypeptide chains (strands) arranged side by
side.
• Has hydrogen bonds between the peptide chains.
• Has R groups above and below the sheet (vertical).
• Is typical of fibrous proteins such as silk.

O H
 Secondary Structure – Triple helix (Superhelix)

- Collagen is the most abundant protein.

- Three polypeptide chains (three α-helix) woven together.

- It is found in connective tissues: bone, teeth, blood

vessels, tendons, and cartilage.

- Consists of glycine (53%), proline (22%), alanine (12%),

and smaller amount of hydroxyproline and hydroxylysine.

- High % of glycine allows the chains to lie close to each

other.

- We need vitamin C to form H-bonding

- (a special enzyme).
 Tertiary Structure

The tertiary structure is determined by attractions and

repulsions between the side chains (R) of the amino acids
in a polypeptide chain.

Interactions between side

chains of the amino acids
fold a protein into a specific
three-dimensional shape.

-S-S-
 Hydrophobic
interactions and
van der Waals
interactions

Polypeptide
backbone

Hydrogen
bond

Disulfide bridge

Ionic bond
 Tertiary Structure
(1) Disulfide (-S-S-)
(2) salt bridge (acid-base)
(3) Hydrophilic (polar)
(4) hydrophobic (nonpolar)
(5) Hydrogen bond
 Tertiary Structure

Shorthand symbols on a protein Ribbon diagram:

Lysozyme (an enzyme)

 Globular proteins

- Have compact, spherical shape.

- Almost soluble in water.

- Carry out the work of the cells:

Synthesis, transport, and metabolism

Myoglobin

Stores oxygen in muscles.

153 amino acids in a single polypeptide chain (mostly α-helix).

 Fibrous proteins

- Have long, thin shape and insoluble in water.

- Involve in the structure of cells and tissues.

α-keratin: skin, nail, hair, and bone

Superhelix:

Collagen

-keratin: feathers of birds

Large amount of -pleated sheet

 Fibrous proteins

α-keratin: hair, wool, skin, and nails

- They are made of two mainly a-helix chains coiled

around each other in a superhelix (supercoil).

- These coils wind around other coils making

larger and stronger structures (like hair).

- α-helix chains bond together by disulfide bond (-S-S-)

- More disulfide bonds, more rigid materials

(horns & nails).

Collagen
 Quaternary Structure

• Occurs when two or more protein units

(polypeptide subunits) combine.
α chain  chain
• Is stabilized by the same interactions found in
tertiary structures (between side chains).

• Hemoglobin consists of four polypeptide

chains as subunits.

• Is a globular protein and transports oxygen in

blood (four molecules of O2).
 chain α chain
• CO is poisonous because it binds 200 times
more strongly to the Fe2+ than does O2 (Cells
can die from lack of O2). Hemoglobin
Summary of Protein Structure
Summary of protein Structure
Examples:
Casein in milk.
Vitellin in egg yolk
 Glycoproteins are proteins which
contain oligosaccharide chains
(glycans) covalently attached to amino acid side-
chains.
 The carbohydrate is attached to the protein in a co-
translational or posttranslational modification.
 This process is known as glycosylation. Secreted
extracellular proteins are often glycosylated.
 In N-glycosylation, sugars are attached to nitrogen,
typically on the amide side-chain of asparagine.
 In O-glycosylation, sugars are attached to oxygen,
typically on serine or threonine, but also
on tyrosine or non-canonical amino acids such
as hydroxylysine & hydroxyproline.
Proteinsconjugated with
Pigments.
Examples:
Haemoglobin.
Cytochromes
Rhodopsin.
Examples:
Iron in Ferretin
Copper in Ceruloplasmin.
Function of proteins
 Denaturation
Active protein
- Is a process of destroying a protein
by chemical and physical means. Ovalbumin

- We can destroy secondary, tertiary,

or quaternary structure but the primary
structure is not affected.

- Denaturing agents: heat, acids and bases,

organic compounds, heavy metal ions, and Denatured protein
mechanical agitation.

- Some denaturations are reversible,

while others permanently damage the protein.
 Denaturation

•Heat: H bonds, Hydrophobic interactions

•Detergents: H bonds

•Acids and bases: Salt bridges, H bonds.

•Reducing agents: Disulfide bonds

•Heavy metal ions (transition metal ions Pb2+, Hg2+): Disulfide

bonds

•Alcohols: H bonds, Hydrophilic interactions

•Agitation: H bonds, Hydrophobic interactions