Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

Protein Science

Volumn 1, Issue 3, 1992, Pages 363-369

  Viitanen, Paul V ^a   Gatenby, Anthony A ^a   Lorimer, George H ^a  

^a DUPONT COMPANY   (United States)

Author keywords

groEL; heat shock proteins; molecular chaperones; protein folding

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN; RIBULOSEBISPHOSPHATE CARBOXYLASE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; ESCHERICHIA COLI; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PURIFICATION;

BACTERIAL PROTEINS; ESCHERICHIA COLI; GROEL PROTEIN; HEAT-SHOCK PROTEINS; KINETICS; METHIONINE; PROTEIN FOLDING; RHODOSPIRILLUM RUBRUM; RIBULOSE-BISPHOSPHATE CARBOXYLASE; SULFUR RADIOISOTOPES;

EID: 0027065105     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560010308     Document Type: Article

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