综述了核磁共振波谱在结构生物学研究中的进展。在溶液中测定生物大分子的结构,分子大小的限制正被减少,尽管新结构的测定仍然需要付出比较大的努力。核磁共振是一个有效的手段,可用于研究在许多细胞过程中存在的弱的或者瞬态的蛋白质-蛋白质相互作用。结构的柔性在蛋白质分子功能中起了中心作用。由于最近方法学的发展,使NMR可以表征蛋白质的动力学,从而可以对分子机制有新的认识。核磁共振波谱可以在原子分辨率下表征无序的蛋白质系统,可以研究折叠路径。跨膜蛋白在细胞中起了关键作用,这使它们成为药物的靶标。应用液体和固体核磁共振技术已经成功测定了跨膜蛋白质的结构。
The recent advances in nuclear magnetic resonance (NMR) spectroscopy used to structural biology were highlighted. The size limitations have been alleviated for the determination of biomolecular structures in solution. Although de novo structure determination still requires considerable effort. NMR also is a highly effective tool for unraveling the atomic details of weak or transient protein-protein interaction that are fundamental to many cellular processes. Structural flexibility plays a central role in the function of protein molecules. 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. NMR can characterize disordered protein ensembles on atomic-level and studying protein folding pathway. Owing to their crucial role in cell function, transmembrane proteins make extremely interesting targets for drugs. Solution and solid-state NMR techniques has been successfully used for determining structures of transmembrane proteins.