GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding

Cell

Volumn 157, Issue 4, 2014, Pages 922-934

  Georgescauld, Florian ^a   Popova, Kristina ^a   Gupta, Amit J ^a   Bracher, Andreas ^a   Engen, John R ^b   Hayer Hartl, Manajit ^a   Hartl, F Ulrich ^a,c  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b NORTHEASTERN UNIVERSITY   (United States)

^c UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN 60; DAPA PROTEIN; EARLY PREGNANCY FACTOR; PROTEIN; UNCLASSIFIED DRUG; PROTEIN DAPA; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; DEUTERIUM HYDROGEN EXCHANGE; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CATALYSIS; CHAPERONIN 10; CHAPERONIN 60; DEUTERIUM EXCHANGE MEASUREMENT; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDRO-LYASES; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOPLASMA SYNOVIAE; OXO-ACID-LYASES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 84900341259     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.03.038     Document Type: Article

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