Publication Abstract from PubMed
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.
Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.,Weingarth M, Ader C, Melquiond AJ, Nand D, Pongs O, Becker S, Bonvin AM, Baldus M Biophys J. 2012 Jul 3;103(1):29-37. PMID:22828329[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
