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偶极波作为蛋白质中螺旋的核磁共振图谱。

Dipolar Waves as NMR maps of helices in proteins.

作者信息

Mesleh Michael F, Opella Stanley J

机构信息

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.

出版信息

J Magn Reson. 2003 Aug;163(2):288-99. doi: 10.1016/s1090-7807(03)00119-8.

DOI:10.1016/s1090-7807(03)00119-8
PMID:12914844
Abstract

Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.

摘要

偶极波描述了蛋白质主链中偶极耦合强度随残基序号的周期性变化。它们在对齐样品中偶极耦合的实验测量与规则二级结构元件中固有的周期性之间提供了直接联系。利用偶极波,可以识别螺旋中的残基和螺旋类型、与理想情况的偏差,还能在完全对齐的样品中确定螺旋相对于外部轴的方向,以及在弱对齐样品的公共框架中确定螺旋之间的相对方向。它们为准确描述螺旋提供了一种工具,也是迈向蛋白质高通量结构测定的重要一步。

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