Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues

Kent Kirshenbaum, Isaac S. Carrico, David A. Tirrell

Research output: Contribution to journalArticlepeer-review


Unnatural amino acids with useful chemical functionality can replace phenylalanine in bacterial proteins. Coexpression of a promiscuous phenylalanine-tRNA synthetase mutant enables the synthesis of target proteins bearing iodophenyl, cyanophenyl, ethynylphenyl, azidophenyl, and pyridyl groups (see general structures). Proteins incorporating the analogues have a range of potential applications, including Pd-mediated conjugation (R=CCH), photoaffinity labeling (R=N3), X-ray phasing (R=I), and novel metal coordination (R=pyridyl).

Original languageEnglish (US)
Pages (from-to)235-237
Number of pages3
Issue number2-3
StatePublished - Mar 1 2002


  • Amino acids
  • Biosynthesis
  • Mutagenesis
  • Photoaffinity labeling
  • Protein modifications

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry


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