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Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity.

Nature methods (2013-08-06)
Zheng Xiang, Haiyan Ren, Ying S Hu, Irene Coin, Jing Wei, Hu Cang, Lei Wang
ABSTRACT

Natural proteins often rely on the disulfide bond to covalently link side chains. Here we genetically introduce a new type of covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine. We demonstrate the utility of this bond for enabling irreversible binding between an affibody and its protein substrate, capturing peptide-protein interactions in mammalian cells, and improving the photon output of fluorescent proteins.

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