Protein backbone 1HN-13Cα and 15N-13Cα residual dipolar and J couplings:: New constraints for NMR structure determination

被引：44

作者：

Ding, KY ^{[1
]}

Gronenborn, AM ^{[1
]}

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 20期

关键词：

D O I：

10.1021/ja049049l

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A simple, sensitivity-enhanced experiment was devised for accurate measurement of backbone 15N-13Cα and 1HN-13Cα couplings in proteins. The measured residual dipolar couplings 2DHCA, 1DNCA, 3DHCA, and 2DNCA for protein GB1 display very good agreement with the refined NMR structure (PDB code: 3GB1. A Karplus-type relationship between the one-bond 1JNCA couplings and the backbone dihedral ψ angles holds, and on the basis of the two-bond 2JNCA couplings a secondary structure index can be established. Copyright © 2003 American Chemical Society.

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页码：6232 / 6233

页数：2

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