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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.

SUBMITTER: Andersson M

PROVIDER: S-EPMC3602767 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Conformational states of melittin at a bilayer interface.

Andersson Magnus M Ulmschneider Jakob P JP Ulmschneider Martin B MB White Stephen H SH

Biophysical journal 20130319 6

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 represe ...[more]

PMID: 23528098

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