Overview of Relaxation Dispersion NMR Spectroscopy to Study Protein Dynamics and Protein-Ligand Interactions
Overview of Relaxation Dispersion NMR Spectroscopy to Study Protein Dynamics and Protein-Ligand Interactions
复制标题
用于研究蛋白质动力学和蛋白质-配体相互作用的弛豫色散核磁共振波谱概述
DOI：
10.1002/cpps.57
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发表时间：
2018
影响因子：
--
通讯作者：
Sugase Kenji
中科院分区：
文献类型：
--
作者：
Walinda Erik;Morimoto Daichi;Sugase Kenji
蛋白质和核酸是所有生物过程的核心。NMR光谱已被证明是优秀的研究这些大分子在不同的时间尺度的动力学。弛豫率和异源核奥弗豪泽效应值可以解析皮科到纳秒时间尺度上的运动，残余偶极耦合提供亚微米到毫秒时间尺度上的信息，甚至可以通过氢交换实验解析几秒到几小时的较慢动力学。弛豫色散实验特别有价值，因为它们可以在微米到毫秒的时间尺度上解析运动，包括与配体结合、酶催化和结构域开放相关的生物分子运动。这些实验提供了结构，动力学和热力学信息的“看不见的”激发构象状态。弛豫色散不仅可以应用于单个生物分子，还可以应用于蛋白质-配体复合物，以研究缔合和解离的动力学和热力学。本文综述了弛豫色散方法学的最新进展，概述了R1 ρ弛豫色散实验，并讨论了它在生物分子相互作用中的应用。John Wiley & Sons，Inc.
Proteins and nucleic acids are central to all biological processes. NMR spectroscopy has proven to be excellent for studying the dynamics of these macromolecules over various timescales. Relaxation rates and heteronuclear nuclear Overhauser‐effect values can resolve motion on pico‐ to nanosecond timescales, residual dipolar couplings provide information on submicro‐ to millisecond timescales, and even slower dynamics over seconds to hours can be resolved by hydrogen‐exchange experiments. Relaxation dispersion experiments are especially valuable because they resolve motion on micro‐ to millisecond timescales, encompassing biomolecular motions associated with ligand binding, enzymatic catalysis, and domain‐domain opening. These experiments provide structural, kinetic, and thermodynamic information on “invisible” excited conformational states. Relaxation dispersion can be applied not only to single biomolecules but also to protein‐ligand complexes to study the kinetics and thermodynamics of association and dissociation. We review recent developments in relaxation dispersion methodology, outline theR1ρrelaxation dispersion experiment, and discuss application to biomolecular interactions. © 2018 by John Wiley & Sons, Inc.