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Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-τc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy

机译：通过溶液NMR光谱法测量先前不可访问的Supra-τc纳秒级至微秒级窗口中的动态和动力学信息

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摘要

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-τc window (defined as τc < supra-τc < 40 μs; in which τc is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-τc window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-τc scale by up to a factor of two (motion up to 25 μs). From the data obtained with these techniques and methodology, the importance of the supra-τc scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-τc scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
机译：核磁共振（NMR）光谱是一种功能强大的工具，它使实验人员能够表征从皮秒到天的各种时间范围内的分子动力学和动力学。这篇综述着重从残余偶极子提取的局部核间矢量动力学的观点着眼于解决先前无法访问的超-τc窗口（定义为τc <超级-τc <40μs；其中τc是分子的整体翻滚时间）。偶联（RDC）和从构象交换的角度通过弛豫色散测量（RD）捕获。第一部分的目的是对如何提取RDC中编码的蛋白质动力学以及如何将此信息与以前无法访问的sup-τc窗口内的蛋白质功能相关联进行详细分析。在第二部分中，分析了RD的最新技术，以及将RD的灵敏度进一步推高至超τc标度达2倍（运动最高25μs）的重大进展。从这些技术和方法学获得的数据来看，随着超τc尺度上的运动与来自实验方的蛋白质功能之间的联系进一步增强，超τc尺度对蛋白质功能和分子识别的重要性变得越来越清晰。分子动力学模拟的结果。

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