title: Solid-state NMR of amyloid membrane interactions.
abstract: Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of "semi-solid" samples, such as the phospholipid vesicles used to study membrane-associated peptides and proteins, which feature prominently in misfolding diseases. Protocols for the preparation of multilamellar vesicles for solid-state NMR studies of Aβ peptides are described, together with procedures for optimization of critical experimental parameters, such as spectral widths, delay times, and field strengths for (31)P, (2)H, and (13)C NMR spectroscopy.
authors.affiliation: School of Chemistry, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia. jgehman@unimelb.edu.au
authors.forename: John D
authors.initials: JD
authors.lastname: Gehman
authors.forename: Frances
authors.initials: F
authors.lastname: Separovic
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010743:Phospholipids / Q000737:chemistry; D011485:Protein Binding
chemical_list: D016229:Amyloid beta-Peptides; D008051:Lipid Bilayers; D010743:Phospholipids