Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues

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

Research output: Contribution to journalArticle

Abstract

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
JournalChemBioChem
Volume3
Issue number2-3
DOIs
StatePublished - Mar 1 2002

Fingerprint

Biosynthesis
Protein Biosynthesis
Phenylalanine
Bearings (structural)
Amino Acyl-tRNA Synthetases
Bacterial Proteins
Labeling
Proteins
Metals
X-Rays
Amino Acids
X rays

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Organic Chemistry
  • Drug Discovery

Cite this

Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues. / Kirshenbaum, Kent; Carrico, Isaac S.; Tirrell, David A.

In: ChemBioChem, Vol. 3, No. 2-3, 01.03.2002, p. 235-237.

Research output: Contribution to journalArticle

Kirshenbaum, Kent ; Carrico, Isaac S. ; Tirrell, David A. / Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues. In: ChemBioChem. 2002 ; Vol. 3, No. 2-3. pp. 235-237.
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