title: NMR structural studies of membrane proteins.
abstract: The three-dimensional structures of membrane proteins are essential for understanding their functions, interactions and architectures. Their requirement for lipids has hampered structure determination by conventional approaches. With optimized samples, it is possible to apply solution NMR methods to small membrane proteins in micelles; however, lipid bilayers are the definitive environment for membrane proteins and this requires solid-state NMR methods. Newly developed solid-state NMR experiments enable completely resolved spectra to be obtained from uniformly isotopically labeled membrane proteins in phospholipid lipid bilayers. The resulting operational constraints can be used for the determination of the structures of membrane proteins.
authors.affiliation: Department of Structural Biology, Wistar Institute, Philadelphia, PA 19104, USA. fmarassi@wistar.upenn.edu
authors.forename: F M
authors.initials: FM
authors.lastname: Marassi
authors.forename: S J
authors.initials: SJ
authors.lastname: Opella
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D002213:Capsid / Q000737:chemistry; D006021:Glycophorins / Q000737:chemistry; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000737:chemistry; D029867:Xenopus Proteins
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D006021:Glycophorins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides; D011950:Receptors, Cholinergic; D029867:Xenopus Proteins; C053300:magainin 1 peptide, Xenopus