ArticleBiophysical journal2012
Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Solid-state NMR spectroscopy reveals unique properties ofCell surface (Amsterdam, Netherlands) · 2025Article
- A Critical Review on Classified Excipient Sodium-Alginate-Based Hydrogels: Modification, Characterization, and Application in Soft Tissue Engineering.Gels (Basel, Switzerland) · 2023Review
- A Structural Model of the Inactivation Gate of Voltage-Activated Potassium Channels.Biophysical journal · 2019Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- A solid view of membrane proteins in situ.Biophysical journal · 2015Article
- Importance of lipid-pore loop interface for potassium channel structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Substrate dynamics in enzyme action: rotations of monosaccharide subunits in the binding groove are essential for pectin methylesterase processivity.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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