Superactivity and conformational changes on α-chymotrypsin upon interfacial binding to cationic micelles

Biochemical Journal

Volumn 378, Issue 3, 2004, Pages 1059-1066

  Celej, M Soledad ^a   D'Andrea, Mariana G ^b   Campana, Patricia T ^c   Fidelio, Gerardo D ^a   Bianconi, M Lucia ^a  

^a UNIVERSIDAD NACIONAL DE CÓRDOBA   (Argentina)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Chymotrypsin; Circular dichroism (CD); Enzyme activation; Fluorescence; Fourier transform infrared (FTIR); Micellar enzymology

Indexed keywords

CATALYSIS; CONFORMATIONS; ENZYMES; FLUORESCENCE; FOURIER TRANSFORM INFRARED SPECTROSCOPY;

CONFORMATION CHANGES; ENZYME STABILITY;

BIOCHEMISTRY;

4 NITROPHENYLACETIC ACID; AROMATIC COMPOUND; CATION; CETRIMIDE; CHYMOTRYPSIN A; PHENYLACETIC ACID DERIVATIVE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME SUBSTRATE; FLUORESCENCE; FOURIER ANALYSIS; INFRARED RADIATION; MICELLE; PRIORITY JOURNAL; PROTEIN INTERACTION; ULTRAVIOLET RADIATION;

CATIONS; CETRIMONIUM COMPOUNDS; CHYMOTRYPSIN; ENZYME ACTIVATION; KINETICS; MICELLES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 1642463952     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031536     Document Type: Article

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