GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II

FEBS Letters

Volumn 411, Issue 1, 1997, Pages 43-47

  Persson, Malin ^a   Carlsson, Uno ^a   Bergenhem, Nils ^b  

^a LINKÖPING UNIVERSITY   (Sweden)

^b UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

Chaperone; GroEL; Human carbonic anhydrase II; Refolding

Indexed keywords

CARBONATE DEHYDRATASE II; CHAPERONIN;

ARTICLE; CONTROLLED STUDY; DRUG INTERACTION; DRUG MIXTURE; ENZYME ACTIVATION; ESCHERICHIA COLI; HUMAN; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS;

CARBONIC ANHYDRASES; ENZYME REACTIVATORS; GROEL PROTEIN; HUMANS; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS;

ARRHENIUS; ESCHERICHIA COLI;

EID: 0030835654     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)00663-7     Document Type: Article

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