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

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.

SUBMITTER: Xiang Z 

PROVIDER: S-EPMC3882359 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature