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Journal Article

Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.

Fulltext (public)

1542193.pdf
(Publisher version), 1004KB

Supplementary Material (public)

1542193-Suppl-1.pdf
(Supplementary material), 2MB

1542193-Suppl-2.zip
(Supplementary material), 2MB

Citation

Weingarth, M., Ader, C., Melquiond, A. J. S., Nand, D., Pong, O., Becker, S., et al. (2012). Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. Biophysical Journal, 103(1), 29-37. doi:10.1016/j.bpj.2012.05.016.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-EEF1-D
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.