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

Humeyra Taskent-Sezgin, Juah Chung, Partha S. Banerjee, Sureshbabu Nagarajan, R. Brian Dyer, Isaac Carrico, Daniel P. Raleigh

Research output: Contribution to journalArticle

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 (US)
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

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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    Taskent-Sezgin, H., Chung, J., Banerjee, P. S., Nagarajan, S., Dyer, R. B., Carrico, I., & Raleigh, D. P. (2010). Azidohomoalanine: A conformationally sensitive IR probe of protein folding protein structure and electrostatics. Angewandte Chemie - International Edition, 49(41), 7473-7475. https://doi.org/10.1002/anie.201003325