Nurgül Bilgin , Jordi C. J. Hintzen , Jasmin Mecinović
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Chemical tools for probing histidine modifications
Histidine is a unique amino acid with critical roles in protein structure and function, ranging from metal ion binding to enzyme catalysis. Histidine residues in proteins also undergo diverse posttranslational modifications, including methylation, phosphorylation and hydroxylation, by various enzymes, some of them being only recently identified and characterised. In this review, we describe the development of chemical tools for understanding the role of histidine residues in chemical and biological systems. We spotlight the application of histidine analogues in probing biomedically important posttranslational modifications of histidine residues in proteins, and we highlight novel bioconjugation methods that enable chemoselective modifications of histidine residues in peptides and proteins.
期刊介绍:
ChemComm (Chemical Communications) is renowned as the fastest publisher of articles providing information on new avenues of research, drawn from all the world''s major areas of chemical research.