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Insight into the interactions, residue snorkeling, and membrane disordering potency of a single antimicrobial peptide into different lipid bilayers - Fig 3

By Majid Jafari (3234825), Faramarz Mehrnejad (3234828) and Farahnoosh Doustdar (3862507)

Abstract

<p><b>The torsion angles of pardaxin residues in the (A) POPG, (B) POPG/POPE (3:1), and (C) POPG/POPE (1:3)</b>. Red dashed lines in the left and right columns show -60 and -45 values, respectively.</p

Topics: Biophysics, Biochemistry, Microbiology, Molecular Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, bend-helix-bend-helix structure, POPC, lipid bilayers, POPG bilayers, cationic residues, C-terminal helix, orientation behavior, membrane disordering potency, membrane-active antimicrobial peptide, peptide-membrane interactions, DMPC, antimicrobial peptides, antimicrobial peptide, lipid bilayer composition, DPPC, lipid bilayers Pardaxin, zwitterionic membranes, MD, phenylalanine residues, residue snorkeling, membrane activity, cationic residues snorkeling, pardaxin snorkeled
Year: 2017
DOI identifier: 10.1371/journal.pone.0187216.g003
OAI identifier: oai:figshare.com:article/5591350
Provided by: FigShare
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