Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain

Biochemistry

Volumn 39, Issue 15, 2000, Pages 4250-4258

  Chen, Jiwen ^a   Smith, David L ^a,b  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; KINETICS; LIGHT SCATTERING; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; DEUTERIUM; DEUTERIUM OXIDE; ESCHERICHIA COLI; GROEL PROTEIN; GUANIDINE; KINETICS; LIGHT; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEPSIN A; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; THERMODYNAMICS; UREA;

ESCHERICHIA COLI;

EID: 0034681907     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992619n     Document Type: Article

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