title: Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.
abstract: Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle within 60-100 degrees, ruling out the possibility of a continuous alpha-helical structure for this protein.
authors.affiliation: Department of Chemistry, University of Minnesota, Minneapolis 55455, USA.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Mascioni
authors.forename: Christine
authors.initials: C
authors.lastname: Karim
authors.forename: Jamillah
authors.initials: J
authors.lastname: Zamoon
authors.forename: David D
authors.initials: DD
authors.lastname: Thomas
authors.forename: Gianluigi
authors.initials: G
authors.lastname: Veglia
mesh_terms: D002135:Calcium-Binding Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D000099211:Phospholamban
chemical_list: D002135:Calcium-Binding Proteins; D000099211:Phospholamban