title: Characterization of membrane protein function by solid-state NMR spectroscopy.
abstract: Membrane proteins are an important class of biological molecules whose association with lipid bilayers and intrinsic molecular mobility can complicate their structural study by high-resolution methods. As different experimental techniques require different membrane mimetics, it can be challenging to relate membrane protein structure to function. This review presents examples of the use of solid-state nuclear magnetic resonance spectroscopy (ssNMR) to correlate structure and function in membrane proteins with diverse biological roles, including signaling, transport, and enzymatic reactions. The types of ssNMR experiments, as well as sources of complementary information and implications for biology, will be discussed. An outlook towards extending ssNMR studies to cellular preparations will be given.
authors.affiliation: NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands.
authors.forename: Lindsay A
authors.initials: LA
authors.lastname: Baker
authors.affiliation: NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands. Electronic address: m.baldus@uu.nl.
authors.forename: Marc
authors.initials: M
authors.lastname: Baldus
mesh_terms: D004798:Enzymes / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D015398:Signal Transduction
chemical_list: D004798:Enzymes; D008565:Membrane Proteins