title: Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.
abstract: Elemental biological functions such as molecular signal transduction are determined by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology methods. We introduce an iterative approach that combines magic-angle spinning solid-state NMR spectroscopy and atomistic molecular dynamics simulations for the determination of the structure and topology of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our study focuses on the Shaker B ball peptide that is representative for rapid N-type inactivating domains of voltage-gated K(+) channels, associated with negatively charged lipid bilayers.
authors: Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.
authors: Markus
authors: M
authors: Weingarth
authors: Christian
authors: C
authors: Ader
authors: Adrien S J
authors: AS
authors: Melquiond
authors: Deepak
authors: D
authors: Nand
authors: Olaf
authors: O
authors: Pongs
authors: Stefan
authors: S
authors: Becker
authors: Alexandre M J J
authors: AM
authors: Bonvin
authors: Marc
authors: M
authors: Baldus
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D047908:Intracellular Signaling Peptides and Proteins; D008051:Lipid Bilayers / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D008051:Lipid Bilayers; D010455:Peptides; D024642:Potassium Channels, Voltage-Gated; C076103:Shaker B inactivating peptide