Fig 3.tif (1.08 MB)
Insight into the interactions, residue snorkeling, and membrane disordering potency of a single antimicrobial peptide into different lipid bilayers - Fig 3
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posted on 2017-11-10, 18:23 authored by Majid Jafari, Faramarz Mehrnejad, Farahnoosh DoustdarThe torsion angles of pardaxin residues in the (A) POPG, (B) POPG/POPE (3:1), and (C) POPG/POPE (1:3). Red dashed lines in the left and right columns show -60 and -45 values, respectively.
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bend-helix-bend-helix structurePOPClipid bilayersPOPG bilayerscationic residuesC-terminal helixorientation behaviormembrane disordering potencymembrane-active antimicrobial peptidepeptide-membrane interactionsDMPCantimicrobial peptidesantimicrobial peptidelipid bilayer compositionDPPClipid bilayers Pardaxinzwitterionic membranesMDphenylalanine residuesresidue snorkelingmembrane activitycationic residues snorkelingpardaxin snorkeled
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