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基于 (13)C(α)- (1)Hα 偶极和羰基化学位移各向异性弛豫相互作用的交叉相关测量骨架二面角 psi 的灵敏脉冲方案。

A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle psi Based on Cross-correlation Between (13)C (alpha)- (1)Halpha Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions.

机构信息

Protein Engineering Network Centers of Excellence and Departments of Molecular and Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, ON, Canada, M5S 1A8.

出版信息

J Biomol NMR. 1998 Feb;11(2):213-20. doi: 10.1023/A:1008284315816.

Abstract

A pulse scheme for measuring cross-correlation between 13Calpha-1Halpha dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle psi is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring psi based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and beta-cyclodextrin.

摘要

提出了一种用于测量 13Calpha-1Halpha 偶极子和羰基化学位移各向异性弛豫机制之间的互相关的脉冲方案,可由此测量蛋白质主链的二面角 psi。与我们最近基于这种互相关效应发表的用于测量 psi 的方案[Yang 等人(1997)J. Am. Chem. Soc.,119,11938-11940]相比,该方法具有显著的灵敏度提高。该方法的实用性通过对 15N、13C 标记的麦芽糖结合蛋白和β-环糊精的 42 kDa 复合物的应用得到了证明。

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