Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.
about
Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.The three lives of viral fusion peptidesMultiple locations of peptides in the hydrocarbon core of gel-phase membranes revealed by peptide (13)C to lipid (2)H rotational-echo double-resonance solid-state nuclear magnetic resonance.Membrane insertion of fusion peptides from Ebola and Marburg viruses studied by replica-exchange molecular dynamics simulations.Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle statepH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.
P2860
Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.
description
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name
Solid-state nuclear magnetic r ...... nd β sheet peptide structures.
@en
type
label
Solid-state nuclear magnetic r ...... nd β sheet peptide structures.
@en
prefLabel
Solid-state nuclear magnetic r ...... nd β sheet peptide structures.
@en
P2093
P2860
P356
P1476
Solid-state nuclear magnetic r ...... nd β sheet peptide structures.
@en
P2093
Charles M Gabrys
David P Weliky
Scott D Schmick
P2860
P304
P356
10.1021/JP312845W
P407
P577
2013-02-28T00:00:00Z