Opella Stanley J
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
J Magn Reson. 2015 Apr;253:129-37. doi: 10.1016/j.jmr.2014.11.015. Epub 2014 Dec 29.
The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects of solid-state NMR, and the chemical shift and homo- and hetero-nuclear dipole-dipole interactions. Solid-state NMR has advanced sufficiently to enable the structures of membrane proteins to be determined under near-native conditions in phospholipid bilayers.
膜蛋白的天然环境是磷脂双分子层。由于该蛋白在核磁共振时间尺度上通过双层膜内的相互作用而固定,因此固态核磁共振方法对于获得高分辨率光谱至关重要。已针对未取向和取向样品开发了相关方法,然而,它们都基于固态核磁共振最基本的方面,即化学位移以及同核和异核偶极-偶极相互作用。固态核磁共振技术已经取得了长足的进步,能够在接近天然的条件下,在磷脂双分子层中确定膜蛋白的结构。