%0 Journal Article
%T Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.
%A Aisenbrey C
%A Salnikov ES
%A Raya J
%A Michalek M
%A Bechinger B
%J Methods Mol Biol
%V 2003
%N 0
%D 2019
%M 31218633
暂无%R 10.1007/978-1-4939-9512-7_23
%X Solid-state NMR spectroscopy has been developed for the investigation of membrane-associated polypeptides and remains one of the few techniques to reveal high-resolution structural information in liquid-disordered phospholipid bilayers. In particular, oriented samples have been used to investigate the structure, dynamics and topology of membrane polypeptides. Much of the previous solid-state NMR work has been developed and performed on peptides but the technique is constantly expanding towards larger membrane proteins. Here, a number of protocols are presented describing among other the reconstitution of membrane proteins into oriented membranes, monitoring membrane alignment by 31P solid-state NMR spectroscopy, investigations of the protein by one- and two-dimensional 15N solid-state NMR and measurements of the lipid order parameters using 2H solid-state NMR spectroscopy. Using such methods solid-state NMR spectroscopy has revealed a detailed picture of the ensemble of both lipids and proteins and their mutual interdependence in the bilayer environment.