Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model

Journal of Molecular Biology

Volumn 291, Issue 3, 1999, Pages 703-713

  Higurashi, Takashi ^a   Nosaka, Koji ^a   Mizobata, Tomohiro ^a   Nagai, Jun ^a   Kawata, Yasushi ^a  

^a TOTTORI UNIVERSITY   (Japan)

Author keywords

cpn10; GroES; Reversible folding transition; Stability; Unfolding and refolding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CHAPERONIN; GUANIDINE; LACTATE DEHYDROGENASE; PROTEIN SUBUNIT;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME INHIBITION; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 0033588259     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2994     Document Type: Article

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