title: Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.
abstract: We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.
authors.affiliation: Center for Insoluble Protein Structures and Department of Chemistry, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus C, Denmark. tv@chem.au.dk
authors.forename: Thomas
authors.initials: T
authors.lastname: Vosegaard
authors.forename: Kresten
authors.initials: K
authors.lastname: Bertelsen
authors.forename: Jan M
authors.initials: JM
authors.lastname: Pedersen
authors.forename: Lea
authors.initials: L
authors.lastname: Thøgersen
authors.forename: Birgit
authors.initials: B
authors.lastname: Schiøtt
authors.forename: Emad
authors.initials: E
authors.lastname: Tajkhorshid
authors.forename: Troels
authors.initials: T
authors.lastname: Skrydstrup
authors.forename: Niels Chr
authors.initials: NC
authors.lastname: Nielsen
mesh_terms: D008565:Membrane Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D013816:Thermodynamics
chemical_list: D008565:Membrane Proteins