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Título

3D-Structure of the interior fusion peptide of HGV/GBV-C by 1H NMR, CD and molecular dynamics studies

Autor Mazzini, Stefania; Fernández-Vidal, Mònica; Galbusera, V.; Castro-Román, F.; Bellucci, M.C; Ragg, E.; Haro Villar, Isabel
Palabras clave Fusion peptides
Hepatitis G virus
E2 envelope protein
Model membranes
Liposomes
NMR spectroscopy
Circular dichroism
Molecular dynamics
Fecha de publicación 6-jun-2007
EditorElsevier
Citación Archives of Biochemistry and Biophysics 465(1): 187-196 (2007)
ResumenIn this work, we present a structural characterization of the putative fusion peptide E2(279–298) corresponding to the E2 envelope protein of the HGV/GBV-C virus by H-1 NMR, CD and MD studies performed in H2O/TFE and in lipid model membranes. The peptide is largely unstructured in water, whereas in H2O/TFE and in model membranes it adopts an helical structure (approximately 65–70%). The partitioning free energy ΔG ranges from -6 to -7.5 kcal mol-1. OCD measurements on peptide-containing hydrated and oriented lipid multilayers showed that the peptide adopts a predominantly surface orientation. The H-1 NMR data (observed NOEs, deuterium exchange rates, Hα chemical shift index and vicinal coupling constants) and the molecular dynamics calculations support the conclusions that the peptide adopts a stable helix in the C-terminal 9–18 residues slightly inserted into the lipid bilayer and a major mobility in the amino terminus of the sequence (1–8 residues).
Descripción 10 pages, 8 figures.-- PMID: 17603997 [PubMed].-- Supplementary information (Figs. S1-S3, tables S1-S2, 3 pages) available at: http://www.sciencedirect.com/science/MiamiMultiMediaURL/B6WB5-4NX2NKW-1/B6WB5-4NX2NKW-1-1/6701/b67d8856b079eefc5f04ac28c2ef05ed/f.doc
Printed version published on Sep 1, 2007.
Versión del editorhttp://dx.doi.org/10.1016/j.abb.2007.05.024
URI http://hdl.handle.net/10261/9870
DOI10.1016/j.abb.2007.05.024
ISSN1096-0384
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