Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.
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Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. / Weingarth, Markus; Ader, Christian; Melquiond, Adrien S J; Nand, Deepak; Pongs, Olaf; Becker, Stefan; Bonvin, Alexandre M J J; Baldus, Marc.
in: BIOPHYS J, Jahrgang 103, Nr. 1, 1, 2012, S. 29-37.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.
AU - Weingarth, Markus
AU - Ader, Christian
AU - Melquiond, Adrien S J
AU - Nand, Deepak
AU - Pongs, Olaf
AU - Becker, Stefan
AU - Bonvin, Alexandre M J J
AU - Baldus, Marc
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
KW - Animals
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Magnetic Resonance Spectroscopy
KW - Molecular Dynamics Simulation
KW - Lipid Bilayers/chemistry
KW - Peptides/chemistry
KW - Potassium Channels, Voltage-Gated/chemistry
KW - Animals
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Magnetic Resonance Spectroscopy
KW - Molecular Dynamics Simulation
KW - Lipid Bilayers/chemistry
KW - Peptides/chemistry
KW - Potassium Channels, Voltage-Gated/chemistry
M3 - SCORING: Journal article
VL - 103
SP - 29
EP - 37
JO - BIOPHYS J
JF - BIOPHYS J
SN - 0006-3495
IS - 1
M1 - 1
ER -