Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy. - Wikidata - awgldk - TriplyDB

Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.

Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.

http://www.wikidata.org/entity/Q37074027

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Membrane protein structure from rotational diffusion Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external region A new understanding of antibiotic action via solid-state NMR of cells with uniform isotopic labeling.Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR.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 ma NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.

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Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.

http://www.wikidata.org/entity/Q37074027

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article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 17 June 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

@en

Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

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type

label

Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

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Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

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prefLabel

Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

@en

Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

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Quantitation of recombinant pr ...... solid-state NMR spectroscopy.

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David P Weliky

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Erica P Vogel

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P2860

The crystal structure of the SIV gp41 ectodomain at 1.47 A resolution

N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil

Solution Structure of Proinsulin: CONNECTING DOMAIN FLEXIBILITY AND PROHORMONE PROCESSING

In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR.

Revealing protein structures in solid-phase peptide synthesis by 13C solid-state NMR: evidence of excessive misfolding for Alzheimer's β.

The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusion

Oritavancin exhibits dual mode of action to inhibit cell-wall biosynthesis in Staphylococcus aureus

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 spectroscopy

Isotopically labeled expression in E. coli, purification, and refolding of the full ectodomain of the influenza virus membrane fusion protein.

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4285-4287

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scholarly article

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10.1021/BI4007034

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25

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2013-06-17T00:00:00Z

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3734946

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