An HNCO-based pulse scheme for the measurement of 13Cα-1Hα one-bond dipolar couplings in 15N, 13C labeled proteins

被引：55
|
作者：
Yang, DW
Tolman, JR
Goto, NK
Kay, LE
机构：
[1] Univ Toronto, Protein Engn Ctr Excellence, Toronto, ON M5S 1A8, Canada
[2] Univ Toronto, Dept Med Genet, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Biochem & Chem, Toronto, ON M5S 1A8, Canada
[4] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
来源：
JOURNAL OF BIOMOLECULAR NMR | 1998年 / 12卷 / 02期
基金：
英国医学研究理事会; 加拿大自然科学与工程研究理事会;
关键词：
C-13(alpha)-H-1(alpha) dipolar couplings; bicelles; HNCO;
D O I：
10.1023/A:1008223017233
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A triple resonance pulse scheme is presented for recording 13C(alpha)-H-1(alpha) one-bond dipolar couplings in N-15, C-13 labeled proteins. HNCO correlation maps are generated where the carbonyl chemical shift is modulated by the C-13(alpha)-H-1(alpha) 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 Bar, 1997a). An application to the protein ubiquitin is described.
引用
收藏
页码：325 / 332
页数：8
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