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NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Chemical Reviews ( IF 62.1 ) Pub Date : 2022-04-21 , DOI: 10.1021/acs.chemrev.1c01023
Aldo R Camacho-Zarco 1 , Vincent Schnapka 1 , Serafima Guseva 1 , Anton Abyzov 1 , Wiktor Adamski 1 , Sigrid Milles 1 , Malene Ringkjøbing Jensen 1 , Lukas Zidek 2, 3 , Nicola Salvi 1 , Martin Blackledge 1
Affiliation  

Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health.

中文翻译:

NMR 提供了对内在无序蛋白质的功能动力学和相互作用的独特见解

本质上无序的蛋白质在所有已知的蛋白质组中无处不在,在细胞和细胞外生物化学的各个方面都发挥着重要作用。要了解它们的功能,有必要确定它们的结构和动态行为,并描述它们相互作用轨迹的物理化学。核磁共振完美地适应了这项任务,提供了报告分子中每个指定共振的整体平均结构和动态参数,揭示了对功能必不可少的反应动力学和热力学的其他无法获得的洞察力。在这篇综述中,我们描述了基于 NMR 的方法在理解构象能量景观、局部和远程动力学的性质和时间尺度以及它们如何依赖于环境方面的最新应用,甚至在牢房里。最后,我们说明了 NMR 揭示对人类健康很重要的功能性无序分子组装的机械基础的能力。
更新日期:2022-04-21
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