{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["103(3)"],"submitter":["Ulmschneider JP"],"pubmed_abstract":["The membrane-active antimicrobial peptide PGLa from Xenopus laevis is known from solid-state (2)H-, (15)N-, and (19)F-NMR spectroscopy to occupy two distinct α-helical surface adsorbed states in membranes: a surface-bound S-state with a tilt angle of ~95° at low peptide/lipid molar ratio (P/L = 1:200), and an obliquely tilted T-state with a tilt angle of 127° at higher peptide concentration (P/L = 1:50). Using a rapid molecular-dynamics insertion protocol in combination with microsecond-scale simulation, we have characterized the structure of both states in detail. As expected, the amphiphilic peptide resides horizontally on the membrane surface in a monomeric form at a low P/L, whereas the T-state is seen in the simulations to be a symmetric antiparallel dimer, with close contacts between"],"journal":["Biophysical journal"],"pagination":["472-482"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3414899"],"repository":["biostudies-literature"],"pubmed_title":["Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations."],"pmcid":["PMC3414899"],"pubmed_authors":["Ulrich AS","Ulmschneider MB","Ulmschneider JP","Smith JC","Strandberg E"],"additional_accession":[]},"is_claimable":false,"name":"Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.","description":"The membrane-active antimicrobial peptide PGLa from Xenopus laevis is known from solid-state (2)H-, (15)N-, and (19)F-NMR spectroscopy to occupy two distinct α-helical surface adsorbed states in membranes: a surface-bound S-state with a tilt angle of ~95° at low peptide/lipid molar ratio (P/L = 1:200), and an obliquely tilted T-state with a tilt angle of 127° at higher peptide concentration (P/L = 1:50). Using a rapid molecular-dynamics insertion protocol in combination with microsecond-scale simulation, we have characterized the structure of both states in detail. As expected, the amphiphilic peptide resides horizontally on the membrane surface in a monomeric form at a low P/L, whereas the T-state is seen in the simulations to be a symmetric antiparallel dimer, with close contacts between","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Aug","modification":"2025-04-04T21:18:07.881Z","creation":"2019-03-27T00:56:32Z"},"accession":"S-EPMC3414899","cross_references":{"pubmed":["22947863"],"doi":["10.1016/j.bpj.2012.06.040"]}}