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Nat Methods. 2013 Sep;10(9):885-8. doi: 10.1038/nmeth.2595. Epub 2013 Aug 4.

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

Author information

1
The Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies, La Jolla, California, USA.

Erratum in

  • Nat Methods. 2014 Feb;11(2):210.

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.

PMID:
23913257
PMCID:
PMC3882359
DOI:
10.1038/nmeth.2595
[Indexed for MEDLINE]
Free PMC Article

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