Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy

被引：65

作者：

Brutscher, B ^{[1
]}

Skrynnikov, NR ^{[1
]}

Bremi, T ^{[1
]}

Brüschweiler, R ^{[1
]}

Ernst, RR ^{[1
]}

机构：

[1] ETH Zentrum, Phys Chem Lab, CH-8092 Zurich, Switzerland

来源：

JOURNAL OF MAGNETIC RESONANCE | 1998年 / 130卷 / 02期

关键词：

nuclear spin relaxation; dipole-CSA cross-correlated relaxation; ZQ/DQ spectroscopy; chemical shielding anisotropy; protein backbone dynamics; anisotropic motion;

D O I：

10.1006/jmre.1997.1312

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A zero-quantum/double-quantum HNCO(H) constant time experiment is presented for the quantitative evaluation of dipole-CSA cross-correlated relaxation involving the H-1(N), N-15, and C-13' nuclei of the peptide plane. A simple procedure that allows the extraction of cross-correlated relaxation rate constants from intensity ratios of well-resolved doublet components along omega(1) is described. The experiment is demonstrated on fully C-13, N-15-labeled ubiquitin. (C) 1998 Academic Press.

引用

页码：346 / 351

页数：6

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