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Direct Visualization of Disulfide Bonds through Diselenide Proxies Using 77 Se NMR Spectroscopy
Author(s) -
Mobli Mehdi,
de Araújo Aline Dantas,
Lambert Lynette K.,
Pierens Gregory K.,
Windley Monique J.,
Nicholson Graham M.,
Alewood Paul F.,
King Glenn F.
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200905206
Subject(s) - disulfide bond , diselenide , nuclear magnetic resonance spectroscopy , chemistry , folding (dsp implementation) , spectroscopy , protein folding , crystallography , stereochemistry , organic chemistry , biochemistry , selenium , physics , quantum mechanics , electrical engineering , engineering
Se‐ing is believing: Many proteins are cross‐braced by disulfide bonds that frequently play key roles in protein structure, folding, and function. Unfortunately, the methods available for assignment of disulfide‐bond connectivities in proteins are technically difficult and prone to misinterpretation. Now disulfide bond connectivities in native proteins can be visualized directly using 77 Se NMR spectroscopy.