Adsorption on montmorillonite prevents oligomerization of Bt Cry1Aa toxin

Journal of Colloid and Interface Science

Volumn 356, Issue 2, 2011, Pages 718-725

  Helassa, N ^a   Revault, M ^b   Quiquampoix, H ^a   Dejardin P ^c   Staunton, S ^a   Noinville, S ^b  

^a UMR ECO SOLS   (France)

^b CNRS   (France)

^c UNIVERSITÉ DE MONTPELLIER   (France)

Author keywords

Bacillus thuringiensis; Conformational change; Cry1Aa toxin; Fourier transform infrared spectroscopy; Oligomerization; Protein adsorption

Indexed keywords

AMIDE I; BACILLUS THURINGIENSIS; CLAY SURFACES; CONFORMATIONAL CHANGE; CONFORMATIONAL FLEXIBILITY; CRY1AA TOXIN; FTIR ABSORPTION; FTIR MEASUREMENTS; PHYLLOSILICATE; PROTEIN ADSORPTION; SECONDARY STRUCTURES; STRENGTH CONDITION; STRUCTURAL CHANGE;

ADSORPTION; AMIDES; BACILLI; BACTERIOLOGY; CLAY MINERALS; DYNAMIC LIGHT SCATTERING; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GEOLOGIC MODELS; IONIC STRENGTH; OLIGOMERIZATION; OLIGOMERS; SILICATE MINERALS; TOXIC MATERIALS;

PROTEINS;

BACTERIAL TOXIN; CRY1AA TOXIN; MONTMORILLONITE; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ADSORPTION; ARTICLE; BACILLUS THURINGIENSIS; CLAY; CONTROLLED STUDY; INFRARED SPECTROSCOPY; IONIC STRENGTH; NONHUMAN; OLIGOMERIZATION; PARTICLE SIZE; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SURFACE PROPERTY;

ADSORPTION; BACILLUS THURINGIENSIS; BENTONITE; HYDROGEN-ION CONCENTRATION; INSECT PROTEINS; PROTEIN CONFORMATION; RECEPTORS, CELL SURFACE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 79952314019     PISSN: 00219797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcis.2011.01.064     Document Type: Article

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