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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, Vol. 103, No. 1, 1, 2012, p. 29-37.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Weingarth, M, Ader, C, Melquiond, ASJ, Nand, D, Pongs, O, Becker, S, Bonvin, AMJJ & Baldus, M 2012, 'Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.', BIOPHYS J, vol. 103, no. 1, 1, pp. 29-37. <http://www.ncbi.nlm.nih.gov/pubmed/22828329?dopt=Citation>

APA

Weingarth, M., Ader, C., Melquiond, A. S. J., Nand, D., Pongs, O., Becker, S., Bonvin, A. M. J. J., & Baldus, M. (2012). Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. BIOPHYS J, 103(1), 29-37. [1]. http://www.ncbi.nlm.nih.gov/pubmed/22828329?dopt=Citation

Vancouver

Weingarth M, Ader C, Melquiond ASJ, Nand D, Pongs O, Becker S et al. Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. BIOPHYS J. 2012;103(1):29-37. 1.

Bibtex

@article{96046a9d791d444aa66d4e12af94be17,
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.",
keywords = "Animals, Amino Acid Sequence, Molecular Sequence Data, Magnetic Resonance Spectroscopy, *Molecular Dynamics Simulation, Lipid Bilayers/chemistry, Peptides/*chemistry, Potassium Channels, Voltage-Gated/chemistry, Animals, Amino Acid Sequence, Molecular Sequence Data, Magnetic Resonance Spectroscopy, *Molecular Dynamics Simulation, Lipid Bilayers/chemistry, Peptides/*chemistry, Potassium Channels, Voltage-Gated/chemistry",
author = "Markus Weingarth and Christian Ader and Melquiond, {Adrien S J} and Deepak Nand and Olaf Pongs and Stefan Becker and Bonvin, {Alexandre M J J} and Marc Baldus",
year = "2012",
language = "English",
volume = "103",
pages = "29--37",
journal = "BIOPHYS J",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "1",

}

RIS

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 -