This document discusses protein denaturation. It defines protein denaturation as the alteration of a protein's native tertiary and quaternary structure due to external stresses like heat, chemicals, or pressure. This disrupts bonds within the protein and can disrupt cell activity or cause cell death. Protein denaturation can be reversible or irreversible depending on if the protein can regain its native structure. Common causes of denaturation include temperature changes, pH changes, oxidation, and enzymatic degradation. Effects include loss of biological activity and changes to size, shape, and physical appearance.

1. PREPARED AND PRESENTED BY:
SAROJ SINGH
MASTERS OF SCIENCE IN BIOTECHNOLOGY

2. • INTRODUCTION
• DEFINITION
• EXAMPLE
• LEVELS OF PROTEIN DENATURATION
• TYPES
• WHAT IS PROTEIN RENATURATION
• CAUSES OF PROTEIN DENATURATION
• EFFECTS OF PROTEIN DENATURATION
• CONCLUSION
• REFERENCE

3. • WHAT IS PROTEIN
• Protein is the most abundantly found
macromolecule of our biological system which is
made up of amino acid residues which are held
together by the help of peptide bond. It
participates in various systems in our body such
as digestive system, reproductive system etc.
• WHAT IS DENATURATION
• Denaturation is the process in which the folding
structure of any molecule is altered due to the
exposure of external stress which may be physical
or chemical.

4. • The process of partial and total alteration in
native, secondary, tertiary and quaternary
structure of protein due to exposure of certain
chemicals and physical factors is called protein
denaturation.
• Denaturation leads break down of various bond
exist within a molecule and macromolecule.
• If protein in a living cell denatured results
disruption of cell activity and possibly cell death.

5. • A classic example of protein denaturation is egg
albumen which get hard and solid due to its
denaturation on high temperature and convert into
white color from its color less appearance.

6. • If a solution containing protein is heated and
treated with some chemical and physical factors
resulting break down of the various bonds
present in secondary, tertiary, quaternary
structure of protein hence protein gets
denatured and convert into its primary
configuration.

7. • In quaternary structure of protein, during protein
denaturation subunits of proteins are dissociated
from each other and get separate.
• In tertiary structure of protein, during protein
denaturation following changes our occurs:
1. Disruption of covalent bond.
2. Disruption of non covalent dipole-dipole bond.
3. Disruption of Vander Val bonds.

8. • In secondary structure of protein, during protein
denaturation protein loss all repeating pattern
such as alpha helix, beta pleated sheets etc.
• In primary structure of protein no changes occur
during denaturation

9. 1). Irreversible denaturation
Some protein after denaturation cannot brought be
back to their native configuration, In that case
denaturation is described as irreversible
denaturation.
2). Reversible denaturation
On the other hand when protein after denaturation
is able to brought back on its native configuration,
in that case denaturation is described as reversible
denaturation.

11. • The process of regaining its
normal properties by
denatured protein is called
protein renaturation. Its occur
when situations are getting
normal which are hardly
responsible for protein
denaturation but the property
of protein denaturation is only
shown by few proteins all the
proteins are not able to
convert in its native
configuration after
denaturation of protein this
type of denaturation is called
reversible denaturation.

12. Denaturation may be brought about by a
variety of agents such as
CHEMICALFACTORS PHYSICALFACTORS

13. 1). Salt concentration:
 Ammonium sulphate
2). Heavy metals:
 Hg++, Ag++,etc.
3). Organic solvent:
 Acetone, alcohol.
4). Detergents:
 Sodium dodecyl sulphate.

14. 1). Mechanical action:
 Shaking, rubbing.
2). TEMPRATURE:
 More than 41°C .
 Frozen temperature.
3). Hydrostatic pressure:
 5000-10,000 atm.
4) Exposure of rays:
 X-Rays, UV-Rays

15. 5). pH:
Change in pH can change the chemistry of
amino acid residues and can lead the
denaturation.
6). Oxidation:
Oxidation of protein can destroy the stability of
protein.
7). Enzymatic degradation:
Protease is an enzyme which is specific to
cleave protein and thus stability of protein will be

16. 1) Possibility to loss biological activity of protein.
2) Decrease in size and shape.
3) Change in its physical appearance.
4) Disruption in its native structure.
5) Disruption in cell activity.
6) Production of toxins by denatured protein.

17. • The process of unfolding of protein is referred as
denaturation thus causing disorganization of the
internal structure of protein which is capable to
block cell activity and possibly leads cell death.
• The process of denaturation may be reversible or
irreversible it is based upon the nature of amino
acid residues which participates in its structure.
• It is caused by some external stress such as
physical and chemical factor which include heat,
exposure of UV-rays, X-rays and certain

18. • J. L. JAIN- FUNDAMENTALS OF
BIOCHEMISTRY.
• ALBERT L. LEHNINGER-BOOK OF
BIOCHEMISTRY.
• WWW.WIKIPEDIA.COM
• OTHER ONLINE SOURCES

19. THANK YOU