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
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container_end_page 7475
container_issue 41
container_start_page 7473
container_title Angewandte Chemie (International ed.)
container_volume 49
creator Taskent-Sezgin, Humeyra
Chung, Juah
Banerjee, Partha S
Nagarajan, Sureshbabu
Dyer, R. Brian
Carrico, Isaac
Raleigh, Daniel P
description 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.
doi_str_mv 10.1002/anie.201003325
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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects 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
title Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics
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