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ISSN (Online) : 2277-4572

CHEMICAL CROSSLINKING OF PROTEINS: A REVIEW

Abstract

Author(s): Hemaprabha. E

Protein-protein interactions comprise the underlying molecular mechanism of a multitude of complex biological processes. Molecular chaperone complexes represent a very good example of multi-protein assemblies where the cooperative action of several components is required for folding/unfolding and transmembrane trafficking of proteins. Signal transduction pathways are illustrative of highly complex protein interaction networks displaying transient and semi-stable association of a series of proteins. Crosslinking is the process of chemically joining two or more molecules by a covalent bond. Crosslinking reagents contain two or more reactive ends that are capable of attaching to specific functional groups (primary amines, sulfhydryls, etc.) on proteins or other molecules.This article describes some of the different crosslinkers and their use in protein protein interactions.