Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions? - Wikidata - awgldk - TriplyDB

Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions?

Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions?

http://www.wikidata.org/entity/Q44864849

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Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants.Differences between CusA and AcrB crystallisation highlighted by protein flexibility.Hydrophobic variations of N-oxide amphiphiles for membrane protein manipulation: importance of non-hydrocarbon groups in the hydrophobic portion.Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation Sulfonated amphipols: synthesis, properties, and applications.Lateral mobility of proteins in liquid membranes revisited.Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study.A new class of amphiphiles bearing rigid hydrophobic groups for solubilization and stabilization of membrane proteins.Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study.Carbohydrate-containing Triton X-100 analogues for membrane protein solubilization and stabilization.An unfolding story of helical transmembrane proteins.Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media for studies of membrane proteins FCS study of the thermodynamics of membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactants Tripod Amphiphiles for Membrane Protein Manipulation.Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies.Micellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head.Hydrophobic variants of ganglio-tripod amphiphiles for membrane protein manipulation.Novel tripod amphiphiles for membrane protein analysis.Folding of diphtheria toxin T-domain in the presence of amphipols and fluorinated surfactants: Toward thermodynamic measurements of membrane protein folding.Use of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization.A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization.Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis.Tandem neopentyl glycol maltosides (TNMs) for membrane protein stabilisation.Engineering a G protein-coupled receptor for structural studies: stabilization of the BLT1 receptor ground state.Improved glucose-neopentyl glycol (GNG) amphiphiles for membrane protein solubilization and stabilization.Resorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stability.An Overview of the Top Ten Detergents Used for Membrane Protein Crystallization

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Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions?

http://www.wikidata.org/entity/Q44864849

description

2004 nî lūn-bûn

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2004年の論文

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2004年學術文章

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Hemifluorinated surfactants: a ...... proteins in aqueous solutions?

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Bernard Pucci

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Cécile Breyton

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Elodie Chabaud

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Jean-Luc Popot

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Yann Chaudier

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P2860

An atypical haem in the cytochrome b(6)f complex

X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases

Structure of the outer membrane protein A transmembrane domain

Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.

Molecular dynamics simulation of n-dodecyl phosphate aggregate structures.

Helical membrane protein folding, stability, and evolution.

Interaction of membrane proteins and lipids with solubilizing detergents.

The hydrophobic effect and the organization of living matter.

Detergents as tools in membrane biochemistry.

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15111115

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