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Protein Classification and Structure Overview

Proteins are classified into fibrous and globular based on their molecular shape, with fibrous proteins being structural and insoluble, while globular proteins are functional and soluble. The structure of proteins is studied at four levels: primary, secondary, tertiary, and quaternary, each describing different aspects of polypeptide chain organization. Denaturation refers to the loss of a protein's native structure and biological activity due to changes in temperature, pH, or hydrogen bonding, affecting secondary and tertiary structures while leaving the primary structure intact.

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5 views8 pages

Protein Classification and Structure Overview

Proteins are classified into fibrous and globular based on their molecular shape, with fibrous proteins being structural and insoluble, while globular proteins are functional and soluble. The structure of proteins is studied at four levels: primary, secondary, tertiary, and quaternary, each describing different aspects of polypeptide chain organization. Denaturation refers to the loss of a protein's native structure and biological activity due to changes in temperature, pH, or hydrogen bonding, affecting secondary and tertiary structures while leaving the primary structure intact.

Uploaded by

chavhanpruthviraj982
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Classification of proteins

Based on their molecular shape

Fibrous protein Globular protein


 Polypeptide chain in the form
 Polypeptide chain in the form
of fibrous
of globular/round
 Secondary structure
 Tertiary structure
 Insoluble in aqueous medium
 Can not be crystallized and elastic  Soluble in aqueous medium
 Can be crystallized
 Insensitive to change in pH
 Sensitive to change in pH
and temperature
and temperature
 Structural protein  Functional protein
Ex: Myosin, Keratin, collagen, elastin, fibrin Ex: Haemoglobin, myoglobin, insulin, enzymes, albumin
Structure of proteins is studied at four different levels
1) Primary
2) secondary
3) tertiary
4) quaternary
Complexity order

Primary structure:

 It describes the sequence of amino acids connected together to form


the polypeptide.
 It may contain more than one chain.
Secondary structure:
 It describes the shape in which polypeptide chain can exist.

 secondary structure arises due to folding of the back bone of the


polypeptide chain to H-bonding.
It can exist in two types
1. α helix
2. β pleated sheets

 Both of these can exist in same protein.

 In α helix, all possible H-bonds are formed to give right handed


screw configuration.
β pleated sheets
 in β pleated sheets, the peptide chains are stretched out to
maximum extension and then joined by intra-molecular H -bonding's.
Tertiary structure:
 It describes overall folding of a polypeptide chain (further
folding of the secondary structure)
 This is due to di-sulphide linkage.
 The function of a protein depends on its tertiary structure.
 If this is disrupted, it loses its activity.
Quaternary structure

 The combination of multiple tertiary structure make quaternary


structure.
 It describes different tertiary structures in a particular spatial
arrangement.
 Some proteins are composed of two or more polypeptide chains
called sub-units.
 The spatial arrangement of sub-units with each other is called
quaternary structure.
Primary Structure
HO

Pr
H 이
Secondary Structure

H 이 H H
C

H이
H
N
C
-C
C--C-N
N
C C C N C
C C
N C N-C C
N
0
C C H
0 0 0 C H
N-C
C N
0 이
H H H
C HO
N C N C C N C C
C H -C
C C C
N
H 0 H 0
이 0
H
H
N C
B-Sheet 0
C

a-Helix

Tertiary Structure Quaternary Structure


Denaturation of protein:

 Native protein is the protein present in a biological system with unique 3-


D structure & biological activity.
 Denaturation is a process in which protein in its native form undergoes
physical changes (i.e, changes in T, pH, H-bonding)
 Due to changes in native protein, globules unfold and helix get uncoiled.
 Hence, protein losses its biological activity.
 During denaturation, 2˚ & 3˚ structures are destroyed and 1 structure
remains intact.

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