Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide.
about
Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayersMembrane protein structure and dynamics from NMR spectroscopy.Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRProperties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusionMembrane fusion induced by vesicular stomatitis virus depends on histidine protonation.The three lives of viral fusion peptidesAn innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies.Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor designTargeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapyTechniques and applications of NMR to membrane proteins.Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopyStructural and functional properties of peptides based on the N-terminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein.Structural Study of a New HIV-1 Entry Inhibitor and Interaction with the HIV-1 Fusion Peptide in Dodecylphosphocholine Micelles.Membrane structure of the human immunodeficiency virus gp41 fusion domain by molecular dynamics simulation.Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion.Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strandHIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopySolid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle stateSolid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups.HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroupsHairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide.Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner.Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations.4-fluorophenylglycine as a label for 19F NMR structure analysis of membrane-associated peptides.Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif.Arabidopsis chloroplast lipid transport protein TGD2 disrupts membranes and is part of a large complex.The effects of alpha-synuclein on phospholipid vesicle integrity: a study using 31P NMR and electron microscopy.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 oCooperativity between the hydrophobic and cross-linking domains of elastin
P2860
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P2860
Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@ast
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@en
type
label
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@ast
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@en
prefLabel
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@ast
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@en
P2093
P356
P1433
P1476
Solid-state nuclear magnetic r ...... ne-bound HIV-1 fusion peptide.
@en
P2093
P304
P356
10.1021/BI0100283
P407
P577
2001-07-01T00:00:00Z