Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

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 significant...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2010-10, Vol.49 (41), p.7473-7475
Hauptverfasser: Taskent-Sezgin, Humeyra, Chung, Juah, Banerjee, Partha S, Nagarajan, Sureshbabu, Dyer, R. Brian, Carrico, Isaac, Raleigh, Daniel P
Format: Artikel
Sprache:eng
Schlagworte:
Alanine - analogs & derivatives
Alanine - chemistry
azidohomoalanine
electrostatics
infrared spectroscopy
Models, Molecular
Protein Conformation
Protein Folding
protein modifications
Protein Structure, Tertiary
Proteins - chemistry
Ribosomal Proteins - chemistry
Spectrophotometry, Infrared - methods
Static Electricity
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Zusammenfassung: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201003325