Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia.
FEBS J. 2011 Mar;278(5):704-15. doi: 10.1111/j.1742-4658.2011.08005.x. Epub 2011 Jan 28.
A strength of NMR spectroscopy is its ability to monitor, on an atomic level, molecular changes and interactions. In this review, which is intended for non-spectroscopist, we describe major uses of NMR in protein science beyond solution structure determination. After first touching on how NMR can be used to quickly determine whether a mutation induces structural perturbations in a protein, we describe the unparalleled ability of NMR to monitor binding interactions over a wide range of affinities, molecular masses and solution conditions. We discuss the use of NMR to measure the dynamics of proteins at the atomic level and over a wide range of timescales. Finally, we outline new and expanding areas such as macromolecular structure determination in multicomponent systems, as well as in the solid state and in vivo.
NMR 光谱学的一个优势在于它能够在原子水平上监测分子变化和相互作用。在这篇面向非光谱学家的综述中,我们描述了 NMR 在蛋白质科学中的除溶液结构测定之外的主要应用。在首先提到 NMR 如何用于快速确定突变是否会引起蛋白质结构的扰动之后,我们描述了 NMR 监测在广泛亲和力、分子量和溶液条件下的结合相互作用的无与伦比的能力。我们讨论了使用 NMR 在原子水平和广泛时间尺度上测量蛋白质动力学的应用。最后,我们概述了新的和扩展的领域,如多组分系统、固态和体内的大分子结构测定。