Isotopically labeled expression in E. coli, purification, and refolding of the full ectodomain of the influenza virus membrane fusion protein.
about
Conformational plasticity of proNGFProduction and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccinesProperly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virusYeast expressed recombinant Hemagglutinin protein of novel H1N1 elicits neutralising antibodies in rabbits and mice.Influence of copy number on the expression levels of pandemic influenza hemagglutinin recombinant protein in methylotrophic yeast Pichia pastoris.Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide maQuantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations.Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopyHIV 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.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 stateSolid-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
Isotopically labeled expression in E. coli, purification, and refolding of the full ectodomain of the influenza virus membrane fusion protein.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Isotopically labeled expressio ...... virus membrane fusion protein.
@en
type
label
Isotopically labeled expressio ...... virus membrane fusion protein.
@en
prefLabel
Isotopically labeled expressio ...... virus membrane fusion protein.
@en
P2093
P2860
P921
P1476
Isotopically labeled expressio ...... virus membrane fusion protein.
@en
P2093
David P Weliky
Jaime Curtis-Fisk
Ryan M Spencer
P2860
P304
P356
10.1016/J.PEP.2008.06.009
P577
2008-06-28T00:00:00Z