tetano
Editor, Senior Moderator
Biophys J. 2012 May 16;102(10):2270-8. Epub 2012 May 15.
The influenza fusion Peptide adopts a flexible flat v conformation in membranes.
L?gar? S, Lag?e P.
Source
D?partement de Biochimie, Microbiologie et Bio-informatique, Institut de Biologie Int?grative et des Syst?mes, and Centre de Recherche sur la Fonction, la Structure et l'Ing?nierie des Prot?ines, Universit? Laval, Quebec City, Quebec, Canada.
Abstract
Knowledge about the influenza fusion peptide (FP) membrane insertion mode is crucial for understanding its fusogenic mechanism. NMR and electron paramagnetic resonance experiments showed that in micelles, the FP inserted as a fixed-angle inverted V. In membranes, however, it was shown to insert as a straight α-helix (by molecular-dynamics simulations) and to adopt multiple kinked conformations (by solid-state NMR). In this work we performed explicit-solvent molecular-dynamics simulations of the influenza FP, and its F9A and W14A mutants, in POPC membranes. The Hα1 chemical shifts predicted from the molecular-dynamics structures are in excellent agreement with the experimental values obtained for the three peptides. The peptide orientation and conformations observed from the simulations lead to a flexible flat-V model in which the peptide lies almost flat on the membrane surface and alternates between kinked and straight-helix conformations.
Copyright ? 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
PMID:
22677380
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22677380
The influenza fusion Peptide adopts a flexible flat v conformation in membranes.
L?gar? S, Lag?e P.
Source
D?partement de Biochimie, Microbiologie et Bio-informatique, Institut de Biologie Int?grative et des Syst?mes, and Centre de Recherche sur la Fonction, la Structure et l'Ing?nierie des Prot?ines, Universit? Laval, Quebec City, Quebec, Canada.
Abstract
Knowledge about the influenza fusion peptide (FP) membrane insertion mode is crucial for understanding its fusogenic mechanism. NMR and electron paramagnetic resonance experiments showed that in micelles, the FP inserted as a fixed-angle inverted V. In membranes, however, it was shown to insert as a straight α-helix (by molecular-dynamics simulations) and to adopt multiple kinked conformations (by solid-state NMR). In this work we performed explicit-solvent molecular-dynamics simulations of the influenza FP, and its F9A and W14A mutants, in POPC membranes. The Hα1 chemical shifts predicted from the molecular-dynamics structures are in excellent agreement with the experimental values obtained for the three peptides. The peptide orientation and conformations observed from the simulations lead to a flexible flat-V model in which the peptide lies almost flat on the membrane surface and alternates between kinked and straight-helix conformations.
Copyright ? 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
PMID:
22677380
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22677380