A genetically encoded fluorescent amino acid

J Am Chem Soc. 2006 Jul 12;128(27):8738-9. doi: 10.1021/ja062666k.

Abstract

The fluorescent amino acid l-(7-hydroxycoumarin-4-yl) ethylglycine 1 has been genetically encoded in E. coli in response to the amber TAG codon. Because of its high fluorescence quantum yield, relatively large Stoke's shift, and sensitivity to both pH and polarity, this amino acid should provide a useful probe of protein localization and trafficking, protein conformation changes, and protein-protein interactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acids / chemistry*
  • Amino Acids / genetics
  • Amino Acids / metabolism
  • Amino Acyl-tRNA Synthetases / biosynthesis
  • Amino Acyl-tRNA Synthetases / chemistry
  • Amino Acyl-tRNA Synthetases / genetics
  • Animals
  • Binding Sites
  • Codon, Terminator
  • Directed Molecular Evolution
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / biosynthesis
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Fluorescence
  • Genetic Code
  • Glycine / analogs & derivatives*
  • Glycine / chemistry
  • Glycine / metabolism
  • Hydrogen-Ion Concentration
  • Molecular Conformation
  • Myoglobin / biosynthesis
  • Myoglobin / chemistry
  • Myoglobin / genetics
  • Protein Biosynthesis
  • RNA, Transfer / biosynthesis
  • RNA, Transfer / chemistry
  • RNA, Transfer / genetics
  • Sperm Whale
  • Umbelliferones / chemistry*
  • Umbelliferones / metabolism

Substances

  • (7-hydroxycoumarin-4-yl) ethylglycine
  • Amino Acids
  • Codon, Terminator
  • Escherichia coli Proteins
  • Myoglobin
  • Umbelliferones
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases
  • Glycine