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各向异性相中残余偶极耦合的精确测量。

Accurate measurement of residual dipolar couplings in anisotropic phase.

作者信息

Cutting Brian, Tolman Joel R, Nanchen Steve, Bodenhausen Geoffrey

机构信息

Institut de Chimie Moléculaire et Biologique, Ecole Polytechnique Fédérale de Lausanne, Switzerland.

出版信息

J Biomol NMR. 2002 Jul;23(3):195-200. doi: 10.1023/a:1019800511340.

DOI:10.1023/a:1019800511340
PMID:12238591
Abstract

The determination of residual dipolar couplings (RDCs) by quantitative J spectroscopy methods such as Heteronuclear Single Quantum Correlation with Phase Encoded Coupling (HSQC-PEC) is prone to systematic errors that may be caused by differential attenuation during the conversion of orthogonal density operator components into observable terms. The attenuation may be caused by miscalibration of radio-frequency pulses and by relaxation effects. A simple method is presented that allows one to remove most of these systematic errors without losses in sensitivity or resolution.

摘要

通过定量J光谱方法(如带有相位编码耦合的异核单量子相关谱,HSQC - PEC)来测定剩余偶极耦合(RDC)容易产生系统误差,这些误差可能是由于在将正交密度算符分量转换为可观测项的过程中存在差异衰减所致。这种衰减可能是由射频脉冲校准错误以及弛豫效应引起的。本文提出了一种简单的方法,该方法能够去除大部分此类系统误差,同时不会损失灵敏度或分辨率。

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本文引用的文献

1
Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra.从简化二维核磁共振谱测量J耦合和偶极耦合
J Magn Reson. 1998 Apr;131(2):373-8. doi: 10.1006/jmre.1998.1361.
2
Measurement of amide 15N-1H one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments.使用手风琴式异核位移相关实验测量蛋白质中的酰胺15N-1H一键耦合。
J Magn Reson B. 1996 Sep;112(3):269-74. doi: 10.1006/jmrb.1996.0141.
3
A quantitative J-correlation experiment for the accurate measurement of one-bond amide 15N-1H couplings in proteins.
一种用于精确测量蛋白质中一键酰胺15N-1H耦合的定量J-相关实验。
J Magn Reson B. 1996 Sep;112(3):245-52. doi: 10.1006/jmrb.1996.0138.