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Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity.
- Source :
-
Nature methods [Nat Methods] 2013 Sep; Vol. 10 (9), pp. 885-8. Date of Electronic Publication: 2013 Aug 04. - Publication Year :
- 2013
-
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.
- Subjects :
- Amino Acid Sequence
Amino Acyl-tRNA Synthetases genetics
Animals
Cysteine chemistry
Cysteine Endopeptidases chemistry
Cysteine Endopeptidases genetics
Cysteine Endopeptidases metabolism
Escherichia coli genetics
Fluorescence
Molecular Sequence Data
Mutation
Phenylalanine chemistry
Photons
Protein Conformation
Proteins genetics
Proteins immunology
Proteins metabolism
Rats
Receptors, Corticotropin-Releasing Hormone genetics
Receptors, Corticotropin-Releasing Hormone metabolism
Recombinant Proteins genetics
Recombinant Proteins immunology
Phenylalanine analogs & derivatives
Protein Engineering methods
Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1548-7105
- Volume :
- 10
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Nature methods
- Publication Type :
- Academic Journal
- Accession number :
- 23913257
- Full Text :
- https://doi.org/10.1038/nmeth.2595