ArticleBiophysical journal2008
Double bilayers and transmembrane gradients: a molecular dynamics study of a highly charged peptide.
Article in Biophysical journal, 2008. 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.
- Efficient Simulations of Solvent Asymmetry Across Lipid Membranes Using Flat-Bottom Restraints.Journal of chemical theory and computation · 2023Article
- The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix.Frontiers in molecular biosciences · 2020Article
- Functional Annotation of Ion Channel Structures by Molecular Simulation.Structure (London, England : 1993) · 2016Article
- Energetics of Multi-Ion Conduction Pathways in Potassium Ion Channels.Journal of chemical theory and computation · 2013Article
- Membrane insertion of a voltage sensor helix.Biophysical journal · 2011Article
- Article
- From the gating charge response to pore domain movement: initial motions of Kv1.2 dynamics under physiological voltage changes.Molecular membrane biology · 2009Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The position and extent of movement of a charged peptide within a membrane bilayer provides much controversy. In our study, we have examined the nature of the highly charged helix-turn-helix motif (S3b and S4) to address how a highly charged peptide is stabilized within a bilayer in the presence of various transmembrane electrical potentials. Our double-bilayer simulation results show how the variation of the salt concentrations between the inner and outer bath establishes a transmembrane potential. Our results also show that important features of the peptide affected by changes in electrical potential are the center of mass depth, the swivel/kink degrees of conformation, and the hydrogen-bonding patterns. As the voltage gradient across the bilayer increased, the center of mass of the peptide shifted in a direction toward the outer bath. The peptide also has a higher percent helical content and the swivel/kink conformation is more rigid for nonpolarized systems where no voltage drop occurred between salt baths. Our results also provide some suggestions for how this domain may be affected by environmental changes as part of the voltage sensor in a K-channel.
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Registered trials
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