ABSTRACT
The formation of either intramolecular or intermolecular covalent crosslinks between amino acid residues in proteins is proving to be an extremely valuable tool in biochemistry with particular use in the study of protein-protein interactions. Naturally occurring inter-and intramolecular crosslinks are commonly found in proteins, the most common being the disulfide bond. One of the more interesting examples of intramolecular cross-linking has involved the use of 1, 3-dibromoacetone. The formation of and subsequent determination of the sites of intrachain or interchain covalent crosslinks provide a direct approach to the study of the folding and interaction of polypeptide chains in solution. Glutaraldehyde should crosslink proteins with the formation of α, ω-Schiff bases, which should be a readily reversible process in the absence of reduction of the Schiff bases with a reducing agent such as sodium borohydride or sodium cyanoborohydride. This is not the case, as summarized by Richards and Knowles.
