Supramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and Molecular Dynamics Simulations

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 iterati...

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Bibliographic Details
Published in:Biophysical journal 2012-07, Vol.103 (1), p.29-37
Main Authors: Weingarth, Markus, Ader, Christian, Melquiond, Adrien S.J., Nand, Deepak, Pongs, Olaf, Becker, Stefan, Bonvin, Alexandre M.J.J., Baldus, Marc
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
lipid bilayers
Lipid Bilayers - chemistry
Lipids
Magnetic Resonance Spectroscopy
Membrane
molecular dynamics
Molecular Dynamics Simulation
Molecular Sequence Data
NMR
Nuclear magnetic resonance
nuclear magnetic resonance spectroscopy
Peptides - chemistry
Polypeptides
potassium channels
Potassium Channels, Voltage-Gated - chemistry
Signal transduction
Simulation
topology
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Summary: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.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2012.05.016