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蛋白质主链H-X偶极相互作用之间的交叉相关弛豫率

Cross-correlated relaxation rates between protein backbone H-X dipolar interactions.

作者信息

Vögeli Beat

机构信息

Department of Biochemistry and Molecular Genetics, University of Colorado Denver, Research Center 1 South, Room 9103, 12801 East 17th Avenue, Aurora, CO, 80045, USA.

出版信息

J Biomol NMR. 2017 Mar;67(3):211-232. doi: 10.1007/s10858-017-0098-5. Epub 2017 Mar 12.

DOI:10.1007/s10858-017-0098-5
PMID:28286915
Abstract

The relaxation interference between dipole-dipole interactions of two separate spin pairs carries structural and dynamics information. In particular, when compared to individual dynamic behavior of those spin pairs, such cross-correlated relaxation (CCR) rates report on the correlation between the spin pairs. We have recently mapped out correlated motion along the backbone of the protein GB3, using CCR rates among and between consecutive H-N and H-C dipole-dipole interactions. Here, we provide a detailed account of the measurement of the four types of CCR rates. All rates were obtained from at least two different pulse sequences, of which the yet unpublished ones are presented. Detailed comparisons between the different methods and corrections for unwanted pathways demonstrate that the averaged CCR rates are highly accurate and precise with errors of 1.5-3% of the entire value ranges.

摘要

两个独立自旋对的偶极-偶极相互作用之间的弛豫干扰携带了结构和动力学信息。特别是,与这些自旋对的个体动力学行为相比,这种交叉相关弛豫(CCR)速率反映了自旋对之间的相关性。我们最近利用连续的H-N和H-C偶极-偶极相互作用之间及内部的CCR速率,描绘了蛋白质GB3主链上的相关运动。在此,我们详细介绍了四种CCR速率的测量方法。所有速率均通过至少两种不同的脉冲序列获得,其中尚未发表的脉冲序列也一并展示。不同方法之间的详细比较以及对不需要的路径的校正表明,平均CCR速率具有很高的准确性和精确性,误差在整个值范围的1.5%至3%之间。

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