title: Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
abstract: It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [13C,15N] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an alpha-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.
authors.affiliation: Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Ovidiu C
authors.initials: OC
authors.lastname: Andronesi
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Karsten
authors.initials: K
authors.lastname: Seidel
authors.forename: Henrike
authors.initials: H
authors.lastname: Heise
authors.forename: Howard S
authors.initials: HS
authors.lastname: Young
authors.forename: Marc
authors.initials: M
authors.lastname: Baldus
mesh_terms: D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary; D012680:Sensitivity and Specificity; D013113:Spin Labels; D013816:Thermodynamics; D000099211:Phospholamban
chemical_list: D002135:Calcium-Binding Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D013113:Spin Labels; D000099211:Phospholamban