title: Conformational states of melittin at a bilayer interface.
abstract: The distribution of peptide conformations in the membrane interface is central to partitioning energetics. Molecular-dynamics simulations enable characterization of in-membrane structural dynamics. Here, we describe melittin partitioning into dioleoylphosphatidylcholine lipids using CHARMM and OPLS force fields. Although the OPLS simulation failed to reproduce experimental results, the CHARMM simulation reported was consistent with experiments. The CHARMM simulation showed melittin to be represented by a narrow distribution of folding states in the membrane interface.
authors.affiliation: Department of Physiology and Biophysics, University of California, Irvine, CA, USA.
authors.forename: Magnus
authors.initials: M
authors.lastname: Andersson
authors.forename: Jakob P
authors.initials: JP
authors.lastname: Ulmschneider
authors.forename: Martin B
authors.initials: MB
authors.lastname: Ulmschneider
authors.forename: Stephen H
authors.initials: SH
authors.lastname: White
mesh_terms: D008051:Lipid Bilayers / Q000737:chemistry; D008555:Melitten / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010713:Phosphatidylcholines / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D008555:Melitten; C017251:1,2-oleoylphosphatidylcholine