Structural highlights
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.
References
- ↑ Weingarth M, Ader C, Melquiond AJ, Nand D, Pongs O, Becker S, Bonvin AM, Baldus M. Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. Biophys J. 2012 Jul 3;103(1):29-37. PMID:22828329 doi:10.1016/j.bpj.2012.05.016
