Conformational stability of muscle acylphosphatase: The role of temperature, denaturant concentration, and pH

Biochemistry

Volumn 37, Issue 5, 1998, Pages 1447-1455

  Chiti, Fabrizio ^a   Van Nuland, Nico A J ^a,c   Taddei, Niccoló ^b   Magherini, Francesca ^b   Stefani, Massimo ^b   Ramponi, Giampietro ^b   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF FLORENCE   (Italy)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE; GLOBULAR PROTEIN; MUSCLE ENZYME; UREA;

ARTICLE; CIRCULAR DICHROISM; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; PH; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS;

ACID ANHYDRIDE HYDROLASES; ANIMALS; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MUSCLE, SKELETAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 0032477888     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971692f     Document Type: Article

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