Reorientation and Dimerization of the Membrane-Bound Antimicrobial Peptide PGLa from Microsecond All-Atom MD Simulations

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 = 1:20...

Full description

Saved in:
Bibliographic Details
Main Authors: Ulmschneider, Jakob P., Smith, Jeremy C., Ulmschneider, Martin B., Ulrich, Anne S., Strandberg, Erik
Format: Artigo
Language:Inglês
Published: The Biophysical Society 2012
Subjects:
Membrane
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3414899/
https://ncbi.nlm.nih.gov/pubmed/22947863
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2012.06.040
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items