Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins

被引：15

作者：

Huang, Jie-rong ^{[1
]}

Ozenne, Valery ^{[1
]}

Jensen, Malene Ringkjobing ^{[1
]}

Blackledge, Martin ^{[1
]}

机构：

[1] Inst Biol Struct Jean Pierre Ebel, CNRS CEA UJF UMR 5075, F-38027 Grenoble, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 02期

关键词：

conformational sampling; intrinsic disorder; NMR spectroscopy; proteins; residual dipolar couplings; INTRINSICALLY DISORDERED PROTEINS; UREA-DENATURED UBIQUITIN; LONG-RANGE ORDER; UNSTRUCTURED PROTEINS; ALPHA-SYNUCLEIN; NATIVE-LIKE; CONFORMATIONS; STATE; ENSEMBLE; SCATTERING;

D O I：

10.1002/anie.201206585

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Conformational analysis: An approach to the prediction of RDCs from disordered protein chains, integrating the effect of nearest neighbors and the alignment characteristics of the statistical coil, is reported. NMR residual dipolar couplings (RDC) are sensitive probes of conformational sampling in unfolded proteins (see picture). Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：687 / 690

页数：4

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