GroEL channels the folding of thioredoxin along one kinetic route

Journal of Molecular Biology

Volumn 314, Issue 5, 2001, Pages 1167-1179

  Bhutani, Nidhi ^a   Udgaonkar, Jayant B ^a  

^a UNIVERSITY OF AGRICULTURAL SCIENCES   (India)

Author keywords

Chaperone; Energy landscape; Folding pathway; GroEL; Thioredoxin

Indexed keywords

CHAPERONIN; POLYPEPTIDE; THIOREDOXIN;

ARTICLE; CONTROLLED STUDY; ENERGY; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; REGULATORY MECHANISM;

ESCHERICHIA COLI;

EID: 0035861988     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.5193     Document Type: Article

References (45)

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7. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP-hydrolysis
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9. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
10. Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
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14. Chaperonin function: Folding by forced unfolding
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24. Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxin
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26. Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding
27. Proline isomerization- independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed α/β protein, Escherichia coli thioredoxin
28. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
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32. Measurement and magnitude of individual rate constants
33. The folding of GroEL-botmd barnase as a model for chaperonin-mediated protein folding
34. Refolding of barnase in the presence of GroE
35. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
36. Effect of GroEL on the re-folding kinetics of α-lactalbumin
37. Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
38. Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry
39. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
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43. Simple, rapid, and quantitative release of periplasmic proteins by chloroform
44. Thioredoxin catalyzes the reduction of insulin disulphides by Dithiotheitol and dihydrolipoamide
45. Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride