Perturbation of conformational dynamics, enzymatic activity, and thermostability of β-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent

Proteins: Structure, Function and Genetics

Volumn 27, Issue 1, 1997, Pages 71-79

  D'Auria, Sabato ^a   Rossi, Mosè ^a   Nucci, Roberto ^a   Irace, Gaetano ^b   Bismuto, Ettore ^b  

^a CNR   (Italy)

^b SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

circular dichroism; frequency domain fluorometry; protein conformational dynamics; thermophilic glycosidase

Indexed keywords

GLYCOSIDASE;

ALKALINITY; ARCHAEBACTERIUM; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME ISOLATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

CIRCULAR DICHROISM; DETERGENTS; ENZYME STABILITY; GLUCOSIDASES; HEAT; HYDROGEN-ION CONCENTRATION; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFOLOBUS;

ARCHAEA; SULFOLOBUS SOLFATARICUS;

EID: 0031031282     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199701)27:1<71::AID-PROT8>3.0.CO;2-Q     Document Type: Article

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