Jain Shefali, Sekhar Ashok
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
J Magn Reson Open. 2022 Jun;10-11:100034. doi: 10.1016/j.jmro.2022.100034.
How proteins switch between various ligand-free and ligand-bound structures has been a key biophysical question ever since the postulation of the Monod-Wyman-Changeux and Koshland-Nemethy-Filmer models over six decades ago. The ability of NMR spectroscopy to provide structural and kinetic information on biomolecular conformational exchange places it in a unique position as an analytical tool to interrogate the mechanisms of biological processes such as protein folding and biomolecular complex formation. In addition, recent methodological developments in the areas of saturation transfer and relaxation dispersion have expanded the scope of NMR for probing the mechanics of transitions in systems where one or more states constituting the exchange process are sparsely populated and 'invisible' in NMR spectra. In this review, we highlight some of the strategies available from NMR spectroscopy for examining the nature of multi-site conformational exchange, using five case studies that have employed NMR, either in isolation, or in conjunction with other biophysical tools.
自从六十多年前提出莫诺德-怀曼-尚热模型和科什兰德-内梅蒂-菲尔默模型以来，蛋白质如何在各种无配体和有配体结合的结构之间转换一直是一个关键的生物物理问题。核磁共振波谱能够提供生物分子构象交换的结构和动力学信息，这使其作为一种分析工具处于独特地位，可用于探究诸如蛋白质折叠和生物分子复合物形成等生物过程的机制。此外，饱和转移和弛豫色散领域最近的方法学发展扩展了核磁共振波谱的范围，用于探测在构成交换过程的一个或多个状态在核磁共振谱中稀疏分布且“不可见”的系统中的转变机制。在这篇综述中，我们重点介绍了核磁共振波谱可用于研究多位点构象交换性质的一些策略，使用了五个单独或与其他生物物理工具结合使用核磁共振波谱的案例研究。
