Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous Insertion.

Perrin, B Scott; Pastor, Richard W

Perrin, B Scott; Pastor, Richard W.

Affiliation

Perrin BS; Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland.
Pastor RW; Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland. Electronic address: pastorr@nhlbi.nih.gov.

Biophys J ; 111(6): 1248-1257, 2016 Sep 20.

Article in En | MEDLINE | ID: mdl-27653483

Subject(s)

Alamethicin/chemistry; Anti-Bacterial Agents/chemistry; Lipid Bilayers/chemistry; Alamethicin/metabolism; Animals; Anti-Bacterial Agents/metabolism; Antimicrobial Cationic Peptides/chemistry; Electromagnetic Fields; Fish Proteins/chemistry; Fishes; Fungal Proteins/chemistry; Fungal Proteins/metabolism; Glycerylphosphorylcholine/analogs & derivatives; Glycerylphosphorylcholine/chemistry; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Phosphatidylcholines; Protein Binding; Protein Conformation, alpha-Helical; Protein Folding; Trichoderma; Viscosity

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Alamethicin / Lipid Bilayers / Anti-Bacterial Agents Limits: Animals Language: En Journal: Biophys J Year: 2016 Document type: Article Country of publication: United States

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