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Azidohomoalanine: A conformationally sensitive IR probe of protein folding protein structure and electrostatics

  • Stony Brook University
  • Emory University

Research output: Contribution to journalArticlepeer-review

87 Scopus citations

Abstract

Highly sensitive: The azido analogue of methionine, azidohomoalanine (see picture), is shown to be a sensitive IR probe of protein structure, folding, and electrostatics, as demonstrated for ribosomal protein NTL9. It can be readily incorporated in to proteins, and the azido frequency is significantly blue-shifted in the thermally unfolded state.

Original languageEnglish
Pages (from-to)7473-7475
Number of pages3
JournalAngewandte Chemie - International Edition
Volume49
Issue number41
DOIs
StatePublished - Oct 4 2010

Keywords

  • Azidohomoalanine
  • Electrostatics
  • Infrared spectroscopy
  • Protein folding
  • Protein modifications

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