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Elsevier, Biophysical Journal, 6(104), p. L12-L14, 2013

DOI: 10.1016/j.bpj.2013.02.006

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Conformational States of Melittin at a Bilayer Interface

Journal article published in 2013 by Magnus Andersson ORCID, Jakob P. Ulmschneider, Martin B. Ulmschneider, Stephen H. White
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This paper is available in a repository.

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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.