The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

Journal of Biological Chemistry

Volumn 273, Issue 18, 1998, Pages 11032-11037

  Veinger, Lea ^a   Diamant, Sophia ^a   Buchner, Johannes ^b   Goloubinoff, Pierre ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; PROTEIN DNAK;

ARTICLE; ESCHERICHIA COLI; HEAT SHOCK; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATE; CHAPERONINS; CHROMATOGRAPHY, GEL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GROEL PROTEIN; HEAT-SHOCK PROTEINS; KINETICS; MUTATION; OXIDATIVE STRESS; PROTEIN DENATURATION; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032079487     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.18.11032     Document Type: Article

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