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首页> 外文期刊>Journal of Molecular Biology >Integrating Non-NMR Distance Restraints to Augment NMR Depiction of Protein Structure and Dynamics
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Integrating Non-NMR Distance Restraints to Augment NMR Depiction of Protein Structure and Dynamics

机译：整合非NMR距离限制以增加蛋白质结构和动力学的NMR描述

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摘要

Nuclear magnetic resonance (NMR) structure refinement is inherently integrative. The refinement incorporates a multitude of experimental data and minimizes the difference between observed and calculated values. Here, we review how the integrative use of non-NMR measurements, in particular, distance restraints from Forster resonance energy transfer and cross-linking coupled with mass spectrometry, can augment NMR depiction of protein structure and dynamics. Refinement against both NMR and non-NMR distance restraints helps to characterize the structures of high-molecular-weight proteins and protein complexes. When a protein fluctuates among multiple conformations at millisecond or a faster timescale, NMR signals from the different conformational states may coalesce into a single set of peaks. The integration of non-NMR distance restraints facilitates the deconvolution of NMR observables to state-specific restraints. Furthermore, the integrative use of fluorescence measurements, which provides an assessment of both length scale and timescale of protein dynamics simplifies protein ensemble structure refinement otherwise with NMR restraints alone and affords a more wholesome picture of protein dynamics. Together, distance measurements are intuitive and easy to implement by using an appropriate pseudoenergy function. Future development shall involve more accurate modeling of paramagnetic and fluorescent probes, incorporation of sparse restraints from new techniques, and characterization of protein structures in a complex cellular environment. (C) 2020 Elsevier Ltd. All rights reserved.
机译：核磁共振（NMR）结构细化本质上是一般的。该细化包含多种实验数据，并最大限度地减少观察到和计算值之间的差异。在这里，我们回顾了来自福尔斯特共振能量转移和与质谱相结合的距离NMR测量的总体距离限制的距离限制，可以增强蛋白质结构和动力学的NMR描绘。针对NMR和非NMR距离限制的细化有助于表征高分子量蛋白和蛋白质复合物的结构。当蛋白质在毫秒或更快的时间尺寸下的多个构象之间波动时，来自不同构象状态的NMR信号可以聚集成一组峰。非NMR距离限制的整合有助于NMR可观察到的核磁共振可观察到的判定限制。此外，荧光测量的整合使用提供了对长度尺度和蛋白质动力学的时间尺度的评估简化了蛋白质集合结构细化，否则单独使用NMR限制，并提供更有益的蛋白质动态图像。在一起，距离测量通过使用适当的伪函数功能直观且易于实现。未来的发展应涉及更准确的顺磁性和荧光探针的建模，从新技术中纳入稀疏约束，并在复杂的细胞环境中表征蛋白质结构。 （c）2020 elestvier有限公司保留所有权利。

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