Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome

Protein Science

Volumn 10, Issue 9, 2001, Pages 1887-1896

  Frankenberg, Rob J ^a   Hsu, Tina S ^b   Yakota, Hisao ^c   Kim, Rosalind ^c   Clark, Douglas S ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b University of California   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

Extremophilic recombinant enzymes; Protein folding; Thermostability

Indexed keywords

PROTEASOME;

ARTICLE; CELL LYSATE; DIFFERENTIAL SCANNING CALORIMETRY; METHANOCOCCUS JANNASCHII; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; SEQUENCE ANALYSIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); METHANOCALDOCOCCUS JANNASCHII; METHANOCOCCUS;

EID: 0034848423     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.05801     Document Type: Article

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