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Protein-Protein Interaction Networks

Proteins are vital macromolecules, the workhorses that facilitate most biological processes at both cellular and systemic levels, but they rarely act alone. Lots of essential molecular processes are carried out by molecular machines that are based on a large number of protein components organized by their Protein-Protein Interactions(PPIs), which refer to intentional physical contacts established between two or more proteins as a result of biochemical events and/or electrostatic forces. Since the interactions are at the core of the entire interactomics system of any living cell, unsurprisingly, specific PPIs are on the basis of multiple diseases.

The result of two or more proteins that interact with a specific functional objective can be demonstrated in several different ways. The measurable effects of protein interactions have been outlined as follows:

Alter the kinetic properties of enzymes
Allow for substrate channeling by moving a substrate between domains or subunits, resulting ultimately in an intended end product
Create a new binding site, typically for small effector molecules
Inactivate or destroy a protein
Change the specificity of a protein for its substrate through the interaction with different binding partners
Serve a regulatory role in either an upstream or a downstream event

Currently, the most popular methods in PPI studies are as follow:

Method PPIs
Co-Immunoprecipitation (co-IP) Stable or strong
Pull-Down Assay Stable or strong
Crosslinking Protein Interaction Analysis Transient or weak
Label Transfer Protein Interaction Analysis Transient or weak
Far-Western Blot Analysis Moderately stable

And Creative Proteomics can provide all the analytical service as described above, and we can help you to interpret the generated data, and visualize the analytical results with bioinformatic tools.


Co-immunoprecipitation (co-IP)
Pull-Down Assay
Crosslinking Protein Interaction Analysis
Label Transfer Protein Interaction Analysis
Far-Western Blot Analysis

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