Proteomics is the study of the structure, function, and interactions of proteins. The proteome is the entire set of proteins expressed by a genome or cell. Proteomics uses various methods to study protein structure and function, qualitative and quantitative analysis of proteins, and protein-protein interactions, which can be stable or transient. Understanding protein interactions is important for studying biological processes and diseases. Proteomics has advantages like identifying biomarkers and drug targets. However, studying proteins is complex due to varying protein concentrations in organisms and cells.

1. Indira Gandhi Krishi
Vishwavidyalaya
College of Agriculture, Raipur
Presentation on-
Proteomics & Protein -Protein
interaction
PRESENTED BY
Pallavi. K
M.Sc.(Pre) Genetics and
Plant Breeding

2. Introduction
● The terms “proteome” and “proteomics” were
coined in the early 1990s by Marc Wilkins, in
order to mirror the terms “genomics” and
“genome”, which represent the entire collection of
genes in an organism.

3. Definitions :
● PROTEOME:
is the complement protein found in the single cell in a
particular environment.
Or
is complete collection of proteins encoded by genome of
an organism.
● PROTEOMICS:
is the study of composition, structure, function and
interaction of the proteins directing the activities of
each living cell.

4. Role of Proteomics
● To study the structure and function of
protein
● To study the 3-D stucture of protein
● Study of qualitative and quantitative
analysis of protein

5. Types of proteomics
● Structural proteomics
Helps to identify newly discovered genes and drug
interaction
● Expression proteomics
Helps to identify the main gene in a particular sample
● Interaction proteomics
It is the pathway in which proteins combined in large
complexes

6. Advantages of study of proteomics
● Shows that genetic alterations are not the reason for all
the types of diseases
● Helps in determining the proper treatment of diseases
● With the help of 3- dimensional analysis of proteins we
have found that HIV protease is the enzyme which is
responsible for AIDS.
● One of the most important use of proteomics in diagnosis
is the identification of biomarkers. The study of drugs in
proteomics is called pharmacoproteomics.

7. Complexities in proteomics
● The study of proteins is very complex
because the concentration of protein is
different in each organism and in each cell
of the organism.

8. Protein-Protein
interactions
● It is physical contacts with molecular
docking between proteins that occur in a
cell or in a living organism.
● Protein -Protein interactions include most
of biological processes like gene
expression, cell growth, proliferation,
nutrient uptake, morphology, motility,
intercellular communication and apoptosis.

9. Types of protein-protein
interaction
1) Stable interaction
2) Transient interaction

10. Stable interaction
● Stable interactions are those which are
purified as multi-subunit complexes, and
the subunits of these complexes can be
identical or different.
● Hemoglobin and core RNA polymerase
are examples of multi-subunit interactions
that form stable complexes.

11. Transient interactions
● These are expected to control the majority of cellular
processes.as the name implies transient interactions are
temporary in nature and typically require a set of
conditions that promote the interaction, such as
phosphorylation, conformational changes or localization
to discrete areas of cell.
● Transient interactions can be strong or weak, and fast or
slow. While in contact with their binding partners,
transiently interacting proteins are involved in wide range
of cellular processes, including protein modification,
transport, folding, signalling and cell cycling.

12. Biological effects of protein-protein
interactions
● The result of two or more proteins that interact with a specific
functional objective can be demonstrated in several different ways.
● After the kinetic properties of enzymes, which may be the result of
subtle changes in substrate binding or allosteric effects.
● Allow for substrate channelling by moving a substrate between
domains or subunits, resulting ultimately in an intended end
product.
● Create new binding sites, typically for small effect or molecules.
● Inactivate or destroy a protein.
● Change the specificity of a protein for its substrate through the
interaction with different binding partners; e.g., demonstrate a new
function that neither a protein an exhibit alone.
● Serve a regulatory role in either an upstream or a downstream
event.

13. Methods to analyze protein-
protein interactions

14. THANK
YOU