波谱学杂志2009，Vol.26Issue(4)：437-456,20.
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
High-Resolution Solid-State NMR Spectroscopy of Membrane Bound Proteins and Peptides Aligned in Hydrated Lipids
傅日强1
作者信息
- 1. Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, Florida, 32310, USA
- 折叠
摘要
Abstract
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.关键词
固体核磁共振/膜蛋白/取向约束/水化磷脂Key words
solid-state NMR/ membrane-bound protein/ orientational constraint/ hydrated lipids分类
数理科学引用本文复制引用
傅日强..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[J].波谱学杂志,2009,26(4):437-456,20.
