Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 15, Pages 11039-11044Publisher
ELSEVIER
DOI: 10.1074/jbc.R109.091306
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Funding
- National Institutes of Health [R01GM062159]
- United States Department of Energy [DE-FG03-00ER46051]
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The ability to genetically encode unnatural amino acids beyond the common 20 has allowed unprecedented control over the chemical structures of recombinantly expressed proteins. Orthogonal aminoacyl-tRNA synthetase/tRNA pairs have been used together with nonsense, rare, or 4-bp codons to incorporate >50 unnatural amino acids into proteins in Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, and mammalian cell lines. This has allowed the expression of proteins containing amino acids with novel side chains, including fluorophores, post-translational modifications, metal ion chelators, photocaged and photocross-linking moieties, uniquely reactive functional groups, and NMR, IR, and x-ray crystallographic probes.
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