Protein Cross-Linking with a Bifunctional Reagent

Definition:

Protein Cross-Linking with a Bifunctional Reagent induces covalent bond formation between adjacent proteins using crosslinkers. The crosslinkers are bifunctional molecules with two reactive ends connected by spacers, typically including disulfide bonds. When a reducing agent is added, the disulfide bonds are cleaved, and the crosslinked pairs are released and can be identified. There are various types of crosslinkers, with the most common being those with photo-reactive groups that become reactive fluorescent probes when exposed to UV light, marking the crosslinked molecules. This technique is widely used to study the spatial relationships, interaction stability, and distance between molecules in protein complexes.

References:

[1]. Fancy DA. Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques. Curr Opin Chem Biol. 2000 Feb;4(1):28-33. [Content Brief]

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