关键词：蛋白质总成;固态核磁共振;魔角旋转;化学位移各向异性重新挂钩;偶极重新挂钩
摘 要：In living organisms, many processes are executed through tightly regulated networks of multi-component macromolecular complexes. Knowledge of structure and dynamics of such assemblies is essential to understanding their biological mechanisms. Solid-state NMR spectroscopy is a prime method for studying macromolecular assemblies, at atomic-level resolution, particularly in systems that are insoluble and lack long-range order. In this report, we review the contemporary magic-angle-spinning (MAS) NMR methods for investigation of proteins assemblies. We describe the progress in multidimensional correlation spectroscopy, recoupling, and decoupling techniques. We discuss emerging methods for recording spectra at MAS frequencies of 40 kHz and faster. We review techniques for sensitivity enhancement and fast data collection. We address isotopic labelling approaches to alleviate spectral congestion, facilitate assignments, and highlight specific intra- and intermolecular interactions. Finally, we present recent case studies on exciting and challenging systems, including assemblies of bacterio-phages and HIV-1 proteins, cytoskeleton-associated proteins, gas vesicles, type Ⅲ secretion system, and protein-RNA complexes.