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OHNO Satoshi
Title

Associate Professor
Department Department of Chemistry and Biomolecular Science
Course Biomolecular Science Course

Research fields

*Site-directed modification of protein via a non-canonical amino acid site-specifically introduced into protein.
The method of chemical modification of protein could be a powerful tool for the investigation of protein structures, functions, interactions, localization and so on. Usually, thiol groups in cysteines or amino groups in lysines are used for the modifications with maleimide derivatives for Cys or succinimidyl ester derivatives for Lys, respectively. However, since these chemical groups are usually found at several sites in proteins, such modifications occur at random sites in protein.
Therefore, our purpose of studies is to develop an effective method for site-specific introduction of a non-canonical amino acid (i.e. not specified in the genetic code) into protein and for site-directed modification of protein via chemoselective chemical reaction with the functional group of the introduced non-canonical amino acid. Site-specifically modified proteins made by our method must facilitate analyses of protein-protein interactions, elucidation of the molecular mechanisms of protein functions and the molecular networks among proteins.

Research Keywords

protein synthesis

protein modification

genetic engineering

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