An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins

被引：0
|
作者：
Daiwen Yang
Joel R. Tolman
Natalie K. Goto
Lewis E. Kay
机构：
[1] University of Toronto,The Protein Engineering Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry
[2] University of Toronto,Department of Biochemistry
来源：
Journal of Biomolecular NMR | 1998年 / 12卷
关键词：
13Cα-1Hα dipolar couplings; bicelles; HNCO;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
A triple resonance pulse scheme is presented for recording 13Cα-1Hα one-bond dipolar couplings in 15N, 13C labeled proteins. HNCO correlation maps are generated where the carbonyl chemical shift is modulated by the 13Cα-1Hα coupling, with the two doublet components separated into individual data sets. The experiment makes use of recently described methodology whereby the protein of interest is dissolved in a dilute solution of bicelles which orient above a critical temperature, thus permitting measurement of significant couplings (Tjandra and Bax, 1997a). An application to the protein ubiquitin is described.
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页码：325 / 332
页数：7
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