Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media for studies of membrane proteins
about
Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants.pH-triggered conformational switching of the diphtheria toxin T-domain: the roles of N-terminal histidines.Partitioning of 2,6-Bis(1H-Benzimidazol-2-yl)pyridine fluorophore into a phospholipid bilayer: complementary use of fluorescence quenching studies and molecular dynamics simulationsCalibration of Distribution Analysis of the Depth of Membrane Penetration Using Simulations and Depth-Dependent Fluorescence Quenching.Thermodynamics of Membrane Insertion and Refolding of the Diphtheria Toxin T-DomainReplacement of C-terminal histidines uncouples membrane insertion and translocation in diphtheria toxin T-domain.Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs.Protein aggregation with poly(vinyl) alcohol surfactant reduces double emulsion-encapsulated mammalian cell-free expression.Membrane Association of the Diphtheria Toxin Translocation Domain Studied by Coarse-Grained Simulations and ExperimentFCS study of the thermodynamics of membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactantsMicellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head.Detergent-activated BAX protein is a monomer.pH-triggered conformational switching along the membrane insertion pathway of the diphtheria toxin T-domainComparison of membrane insertion pathways of the apoptotic regulator Bcl-xL and the diphtheria toxin translocation domain.Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi.Folding of diphtheria toxin T-domain in the presence of amphipols and fluorinated surfactants: Toward thermodynamic measurements of membrane protein folding.Conformational switching of the diphtheria toxin T domain.Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state.Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain.The pH-Dependent Trigger in Diphtheria Toxin T Domain Comes with a Safety Latch.Refining Protein Penetration into the Lipid Bilayer Using Fluorescence Quenching and Molecular Dynamics Simulations: The Case of Diphtheria Toxin Translocation Domain.
P2860
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P2860
Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media for studies of membrane proteins
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
Interactions of fluorinated su ...... r studies of membrane proteins
@en
type
label
Interactions of fluorinated su ...... r studies of membrane proteins
@en
prefLabel
Interactions of fluorinated su ...... r studies of membrane proteins
@en
P2093
P2860
P1433
P1476
Interactions of fluorinated su ...... r studies of membrane proteins
@en
P2093
Alexey S Ladokhin
Bernard Pucci
Christiane Contino-Pépin
Joshua Brettmann
Mykola V Rodnin
Yevgen O Posokhov
P2860
P304
P356
10.1529/BIOPHYSJ.107.126235
P407
P577
2008-02-29T00:00:00Z