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Nature Research, Nature Methods, 9(10), p. 885-888, 2013

DOI: 10.1038/nmeth.2595

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

Journal article published in 2013 by Zheng Xiang, Haiyan Ren, Ying S. Hu, Irene Coin, Jing Wei, Hu Cang, Lei Wang ORCID
This paper is available in a repository.
This paper is available in a repository.

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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.