Mittermaier Anthony, Kay Lewis E
Department of Chemistry, McGill University, Montreal, Quebec H3A 2K6, Canada.
Science. 2006 Apr 14;312(5771):224-8. doi: 10.1126/science.1124964.
There is growing evidence that structural flexibility plays a central role in the function of protein molecules. Many of the experimental data come from nuclear magnetic resonance (NMR) spectroscopy, a technique that allows internal motions to be probed with exquisite time and spatial resolution. Recent methodological advancements in NMR have extended our ability to characterize protein dynamics and promise to shed new light on the mechanisms by which these molecules function. Here, we present a brief overview of some of the new methods, together with applications that illustrate the level of detail at which protein motions can now be observed.
越来越多的证据表明，结构灵活性在蛋白质分子的功能中起着核心作用。许多实验数据来自核磁共振（NMR）光谱学，这是一种能够以极高的时间和空间分辨率探测内部运动的技术。NMR最近的方法学进展扩展了我们表征蛋白质动力学的能力，并有望为这些分子发挥功能的机制提供新的见解。在这里，我们简要概述一些新方法，以及说明现在可以观察到蛋白质运动细节程度的应用。
