title: Solid-state NMR and membrane proteins.
abstract: 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.
authors: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: sopella@ucsd.edu.
authors: Stanley J
authors: SJ
authors: Opella
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010743:Phospholipids / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013113:Spin Labels
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids; D013113:Spin Labels
keywords: Bilayers; Chemical shift anisotropy; Dipolar coupling; Magic angle spinning; Phospholipids; Structure determination