Journal
NATURE METHODS
Volume 10, Issue 9, Pages 885-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.2595
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Funding
- Nomis Postdoctoral Fellowship
- European Commission
- California Institute for Regenerative Medicine [RN1-00577-1]
- US National Institutes of Health [1DP20D004744-01, P30CA014195]
- NATIONAL CANCER INSTITUTE [P30CA014195] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [DP2OD004744] Funding Source: NIH RePORTER
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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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