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

2010; Wiley; Volume: 49; Issue: 41 Linguagem: Inglês

10.1002/anie.201003325

1521-3773

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

Photosynthetic Processes and Mechanisms

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. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.