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

Humeyra Taskent-Sezgin, Juah Chung, Partha 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
Externally publishedYes

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Protein folding
Electrostatics
Proteins
Ribosomal Proteins
Methionine
azidohomoalanine

Keywords

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

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Azidohomoalanine : A conformationally sensitive IR probe of protein folding protein structure and electrostatics. / Taskent-Sezgin, Humeyra; Chung, Juah; Banerjee, Partha; Nagarajan, Sureshbabu; Dyer, R. Brian; Carrico, Isaac; Raleigh, Daniel P.

In: Angewandte Chemie - International Edition, Vol. 49, No. 41, 04.10.2010, p. 7473-7475.

Research output: Contribution to journalArticle

Taskent-Sezgin, Humeyra ; Chung, Juah ; Banerjee, Partha ; Nagarajan, Sureshbabu ; Dyer, R. Brian ; Carrico, Isaac ; Raleigh, Daniel P. / Azidohomoalanine : A conformationally sensitive IR probe of protein folding protein structure and electrostatics. In: Angewandte Chemie - International Edition. 2010 ; Vol. 49, No. 41. pp. 7473-7475.
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