Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. - Wikidata - thesis-toulmin - TriplyDB

Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

http://www.wikidata.org/entity/Q34412679

about

Sorting signal of Escherichia coli OmpA is modified by oligo-(R)-3-hydroxybutyrate Membrane proteins: always an insoluble problem?Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET A saposin-lipoprotein nanoparticle system for membrane proteins.Steroid-based facial amphiphiles for stabilization and crystallization of membrane proteins.Three-dimensional structure of human γ-secretase Application of amphipols for structure-functional analysis of TRP channels.High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase Structural basis of Smoothened regulation by its extracellular domains Structuring detergents for extracting and stabilizing functional membrane proteins Designer lipid-like peptides: a class of detergents for studying functional olfactory receptors using commercial cell-free systems Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics.Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus.Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35.NMR study of a membrane protein in detergent-free aqueous solution.Solid state NMR: The essential technology for helical membrane protein structural characterization.APols-aided protein precipitation: a rapid method for concentrating proteins for proteomic analysis.Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis Sequence-specific dimerization of a transmembrane helix in amphipol A8-35.The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation Single-particle electron microscopy in the study of membrane protein structure Electron cryomicroscopy of membrane proteins: specimen preparation for two-dimensional crystals and single particles.Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy Design, synthesis, and properties of branch-chained maltoside detergents for stabilization and crystallization of integral membrane proteins: human connexin 26.Structure and dynamic properties of membrane proteins using NMR.Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.Synthesis, characterization and applications of a perdeuterated amphipol.The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.Labeling and functionalizing amphipols for biological applications.Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: a biochemical and structural case study.Amphipol-mediated screening of molecular orthoses specific for membrane protein targets.Efficient protein production inspired by how spiders make silk The use of amphipathic polymers for cryo electron microscopy of NADH:ubiquinone oxidoreductase (complex I).An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump Increased immunoaccessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with Chlamydia muridarum.Hydrophobic variations of N-oxide amphiphiles for membrane protein manipulation: importance of non-hydrocarbon groups in the hydrophobic portion.

P2860

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P2860

Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

http://www.wikidata.org/entity/Q34412679

description

1996 nî lūn-bûn

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1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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name

Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Proceedings of the National Academy of Sciences of the United States of America

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Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.

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Audebert R

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Popot JL

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Bacteriorhodopsin and related pigments of halobacteria

Solubilization of membranes by detergents.

Membrane solubilization by a hydrophobic polyelectrolyte: surface activity and membrane binding

Characterization of the chloroplast cytochrome b6f complex as a structural and functional dimer.

SOME NEW STRUCTURAL ASPECTS AND OLD CONTROVERSIES CONCERNING THE CYTOCHROME b6f COMPLEX OF OXYGENIC PHOTOSYNTHESIS.

Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins.

Secondary electron transfer in reaction centers of Rhodopseudomonas sphaeroides. Out-of-phase periodicity of two for the formation of ubisemiquinone and fully reduced ubiquinone.

Purification of bacteriorhodopsin and characterization of mature and partially processed forms.

Solubilization of membranes by detergents

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15047-15050

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scholarly article

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