Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.
about
Magic angle spinning NMR of virusesFusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.Multiple 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.REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion CatalysisHIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Computer-Aided Approaches for Targeting HIVgp41.The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.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.Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.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 stateMolecular dynamics simulations and conductance studies of the interaction of VP1 N-terminus from Polio virus and gp41 fusion peptide from HIV-1 with lipid membranes.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.Solid-state nuclear magnetic resonance (NMR) spectroscopy of human immunodeficiency virus gp41 protein that includes the fusion peptide: NMR detection of recombinant Fgp41 in inclusion bodies in whole bacterial cells and structural characterization o
P2860
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P2860
Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
Major antiparallel and minor p ...... ficiency virus fusion peptide.
@en
type
label
Major antiparallel and minor p ...... ficiency virus fusion peptide.
@en
prefLabel
Major antiparallel and minor p ...... ficiency virus fusion peptide.
@en
P2860
P356
P1433
P1476
Major antiparallel and minor p ...... ficiency virus fusion peptide.
@en
P2093
David P Weliky
Scott D Schmick
P2860
P304
10623-10635
P356
10.1021/BI101389R
P407
P577
2010-11-24T00:00:00Z