ArticleBiophysical journal1999
Alamethicin helices in a bilayer and in solution: molecular dynamics simulations.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
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- Thermal Friction Enhancement in Zwitterionic Monolayers.The journal of physical chemistry. C, Nanomaterials and interfaces · 2022Article
- Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.The journal of physical chemistry letters · 2021Article
- Glucose Can Protect Membranes against Dehydration Damage by Inducing a Glassy Membrane State at Low Hydrations.Membranes · 2019Article
- Folding a viral peptide in different membrane environments: pathway and sampling analyses.Journal of biological physics · 2018Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Structural Behavior of the Peptaibol Harzianin HK VI in a DMPC Bilayer: Insights from MD Simulations.Biophysical journal · 2017Article
- Composition and Activity of the Non-canonical Gram-positive SecY2 Complex.The Journal of biological chemistry · 2016Article
- Molecular Dynamics Simulations of Amyloid β-Peptide (1-42): Tetramer Formation and Membrane Interactions.Biophysical journal · 2016Article
- Multiscale modeling of droplet interface bilayer membrane networks.Biomicrofluidics · 2015Article
- Analysis of the flexibility and stability of the structure of magainin in a bilayer, and in aqueous and nonaqueous solutions using molecular dynamics simulations.Journal of molecular modeling · 2015Article
- Asymmetric binding to NS5A by daclatasvir (BMS-790052) and analogs suggests two novel modes of HCV inhibition.Journal of medicinal chemistry · 2014Article
- Pore dynamics and conductance of RyR1 transmembrane domain.Biophysical journal · 2014Article
- More than the sum of its parts: coarse-grained peptide-lipid interactions from a simple cross-parametrization.The Journal of chemical physics · 2014Article
- A thermodynamic approach to alamethicin pore formation.Biochimica et biophysica acta · 2014Article
- Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations.International journal of molecular sciences · 2013Article
- Extracting curvature preferences of lipids assembled in flat bilayers shows possible kinetic windows for genesis of bilayer asymmetry and domain formation in biological membranes.The Journal of membrane biology · 2013Article
- Construction and validation of a homology model of the human voltage-gated proton channel hHV1.The Journal of general physiology · 2013Article
- The dimerization interface of the glycoprotein Ibβ transmembrane domain corresponds to polar residues within a leucine zipper motif.Protein science : a publication of the Protein Society · 2011Article
3 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
Alamethicin is an alpha-helical channel-forming peptide, which inserts into lipid bilayers in a voltage-dependent, asymmetrical fashion. Nanosecond molecular dynamics simulations have been used to compare alamethicin conformation and dynamics in three different environments: 1) in water; 2) in methanol; and 3) inserted into a lipid (palmitoyl-oleoyl-phosphatidylcholine) bilayer to form a transmembrane helix. In the bilayer and in methanol, there was little change (Calpha RMSD approximately 0.2 nm over 2 ns and 1 ns) from the initial helical conformation of the peptide. In water there were substantial changes (Calpha RMSD approximately 0.4 nm over 1 ns), especially in the C-terminal segment of the peptide, which lost its alpha-helical conformation. In the bilayer and in methanol, the alamethicin molecule underwent hinge-bending motion about its central Gly-X-X-Pro sequence motif. Analysis of H-bonding interactions revealed that the polar C-terminal side chains of alamethicin provided an "anchor" to the bilayer/water interface via formation of multiple H-bonds that persisted throughout the simulation. This explains why the preferred mode of helix insertion into the bilayer is N-terminal, which is believed to underlie the asymmetry of voltage activation of alamethicin channels.
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