Solution and membrane-bound chaperone activity of the diphtheria toxin translocation domain towards the catalytic domain

FEBS Journal

Volumn 278, Issue 23, 2011, Pages 4516-4525

  Chassaing, Anne ^a   Pichard, Sylvain ^a   Araye Guet, Anne ^a   Barbier, Julien ^a   Forge, Vincent ^b   Gillet, Daniel ^a  

^a SERVICE DE CHIMIE BIOORGANIQUE ET DE MARQUAGE   (France)

^b DIF   (France)

Author keywords

diphtheria toxin; membrane interaction; molten globule; protein folding; translocation

Indexed keywords

CHAPERONE; DIPHTHERIA TOXIN; RECOMBINANT PROTEIN;

ARTICLE; BINDING AFFINITY; BIOCATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; FLUORESCENCE SPECTROSCOPY; GENE INSERTION; MEMBRANE PERMEABILITY; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN TRANSPORT; TOXIN STRUCTURE;

CATALYTIC DOMAIN; CYTOPLASM; DIPHTHERIA TOXIN; HYDROGEN-ION CONCENTRATION; MOLECULAR CHAPERONES; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN TRANSPORT; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; UNILAMELLAR LIPOSOMES;

EID: 81055136733     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08053.x     Document Type: Article

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