Thermodynamics and kinetics of folding of common-type acylphosphatase: Comparison to the highly homologous muscle isoenzyme

Biochemistry

Volumn 38, Issue 7, 1999, Pages 2135-2142

  Taddei, Niccolò ^b   Chiti, Fabrizio ^c   Paoli, Paolo ^b   Fiaschi, Tania ^b   Bucciantini, Monica ^b   Stefani, Massimo ^b   Dobson, Christopher M ^c   Ramponi, Giampietro ^a,b  

^a Department of Biochemical Sciences ^*  (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE; ISOENZYME;

ARTICLE; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; ENZYME KINETICS; EQUILIBRIUM CONSTANT; FLUORESCENCE ANALYSIS; IONIC STRENGTH; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ACID ANHYDRIDE HYDROLASES; ENZYME STABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; ISOENZYMES; KINETICS; MUSCLE PROTEINS; OSMOLAR CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 0033573838     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9822630     Document Type: Article

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