水化磷脂层中蛋白质和多肽的高分辨固体核磁共振波谱学

有序样品的固体核磁共振(NMR)已快速发展成测定蛋白质和多肽在“仿真”水化磷脂层中高分辨结构的重要谱学方法. 由于与膜相连的蛋白质和多肽的结构、动力学和功能往往都和其周边自然环境密切相关，因此人们把蛋白质和多肽有序排列于水化磷脂层中进行固体NMR测量, 从而获得与取向相关的各向异性自旋相互作用. 这些取向约束可作为结构参数重构蛋白质在水化磷脂层中的高分辨三维结构. 近十年来在样品制备，NMR探头和实验方法方面的显著发展，极大地促进了有序样品的固体NMR的发展，并使之成为测定与膜相连的蛋白质和多肽结构的有效方法. 该综述介绍有序样品的固体NMR谱学方法，并总结此领域里的最新研究进展.

High-Resolution Solid-State NMR Spectroscopy of Membrane Bound Proteins and Peptides Aligned in Hydrated Lipids

Solid-state nuclear magnetic resonance (NMR) of aligned samples has been rapidly emerged as a successful and important spectroscopic approach for high-resolution structural characterization of membrane-bound proteins and peptides in their "native-like" hydrated lipid bilayers. Because the structures, dynamics, and functions of membrane-bound proteins and peptides are highly associated with heterogeneous native environments, proteins and peptides are prepared for solid-state NMR measurements in the presence of either bilayers that are mechanically aligned on glass plates or magnetically aligned bicelles. Orientation dependent anisotropic spin nuclear interactions from these aligned proteins and peptides can be obtained. These orientational restraints can be assembled into high-resolution three-dimensional structures. Driven by significant advances in sample preparation protocols as well as NMR probes and other methodology developments in the past decade, the aligned sample NMR approach has been well developed and become an effective way for structural characterization of membrane-bound proteins and peptides. This review introduces high resolution solid-state NMR spectroscopy of aligned samples and summarizes recent methodology developments in this arena.