title: Solid-state NMR approaches to study protein structure and protein-lipid interactions.
abstract: 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 (31)P solid-state NMR spectroscopy; investigations of the protein by one- and two-dimensional (15)N solid-state NMR; and measurements of the lipid order parameters using (2)H 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.
authors: Institut de chimie, CNRS, Université de Strasbourg, UMR 7177, Strasbourg, France.
authors: Christopher
authors: C
authors: Aisenbrey
authors: Matthias
authors: M
authors: Michalek
authors: Evgeniy S
authors: ES
authors: Salnikov
authors: Burkhard
authors: B
authors: Bechinger
mesh_terms: D003902:Detergents / Q000494:pharmacology; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D050356:Lipid Metabolism / Q000187:drug effects; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008863:Microspheres; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D011522:Protons; D015203:Reproducibility of Results; D012995:Solubility; D013010:Sonication; D014867:Water / Q000737:chemistry
chemical_list: D003902:Detergents; D008051:Lipid Bilayers; D011506:Proteins; D011522:Protons; D014867:Water