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本文引用的文献

1
Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein.对在一个PDZ结构域蛋白中结合时表现出结构和动力学变化的两个残基网络的映射。
J Am Chem Soc. 2008 Jul 16;130(28):8931-9. doi: 10.1021/ja0752080. Epub 2008 Jun 18.
2
Quantitative lid dynamics of MDM2 reveals differential ligand binding modes of the p53-binding cleft.MDM2的定量盖子动力学揭示了p53结合裂隙的不同配体结合模式。
J Am Chem Soc. 2008 May 21;130(20):6472-8. doi: 10.1021/ja800201j. Epub 2008 Apr 25.
3
On the measurement of 15N-{1H} nuclear Overhauser effects.关于15N-{1H}核Overhauser效应的测量
J Magn Reson. 2008 Jun;192(2):302-13. doi: 10.1016/j.jmr.2008.03.011. Epub 2008 Mar 23.
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A hierarchy of timescales in protein dynamics is linked to enzyme catalysis.蛋白质动力学中的时间尺度层次结构与酶催化作用相关联。
Nature. 2007 Dec 6;450(7171):913-6. doi: 10.1038/nature06407. Epub 2007 Nov 18.
5
An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange.一种无交换的15N横向弛豫测量方法:核磁共振波谱在研究具有普遍化学交换的折叠中间体中的应用。
J Am Chem Soc. 2007 Sep 19;129(37):11468-79. doi: 10.1021/ja072717t. Epub 2007 Aug 28.
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Conformational entropy in molecular recognition by proteins.蛋白质分子识别中的构象熵。
Nature. 2007 Jul 19;448(7151):325-9. doi: 10.1038/nature05959.
7
Model-free analysis for large proteins at high magnetic field strengths.高磁场强度下大蛋白质的无模型分析。
J Biomol NMR. 2007 Aug;38(4):315-24. doi: 10.1007/s10858-007-9171-9. Epub 2007 Jun 26.
8
Protein backbone dynamics through 13C'-13Calpha cross-relaxation in NMR spectroscopy.核磁共振波谱中通过13C'-13Cα交叉弛豫研究蛋白质主链动力学
J Am Chem Soc. 2006 Aug 30;128(34):11072-8. doi: 10.1021/ja0600577.
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Temperature dependence of NMR order parameters and protein dynamics.核磁共振序参量与蛋白质动力学的温度依赖性
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NMR characterization of the dynamics of biomacromolecules.生物大分子动力学的核磁共振表征
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在存在交叉相关弛豫的情况下,通过稳态(15)N-{(1)H}核Overhauser效应测量对蛋白质中的高频运动进行精确采样。

Accurate sampling of high-frequency motions in proteins by steady-state (15)N-{(1)H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation.

作者信息

Ferrage Fabien, Cowburn David, Ghose Ranajeet

机构信息

New York Structural Biology Center, New York, New York 10027, USA.

出版信息

J Am Chem Soc. 2009 May 6;131(17):6048-9. doi: 10.1021/ja809526q.

DOI:10.1021/ja809526q
PMID:19358609
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3547682/
Abstract

The steady-state {(1)H}-(15)N NOE experiment is used in most common NMR analyses of backbone dynamics to accurately ascertain the effects of the fast dynamic modes. We demonstrate here that, in its most common implementation, this experiment generates an incorrect steady state in the presence of CSA/dipole cross-correlated relaxation leading to large errors in the characterization of these high-frequency modes. This affects both the quantitative and qualitative interpretation of (15)N backbone relaxation in dynamic terms. We demonstrate further that minor changes in the experimental implementation effectively remove these errors and allow a more accurate interpretation of protein backbone dynamics.

摘要

稳态{(1)H}-(15)N NOE实验用于大多数常见的主链动力学NMR分析,以准确确定快速动力学模式的影响。我们在此证明,在其最常见的实施方式中,该实验在存在CSA/偶极子交叉相关弛豫的情况下会产生不正确的稳态,从而导致在表征这些高频模式时出现大的误差。这在动力学方面影响了(15)N主链弛豫的定量和定性解释。我们进一步证明,实验实施中的微小变化有效地消除了这些误差,并允许对蛋白质主链动力学进行更准确的解释。