A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar

Journal of Molecular Biology

Volumn 297, Issue 5, 2000, Pages 1037-1044

  Bhutani, Nidhi ^a   Udgaonkar, Jayant B ^a  

^a UNIVERSITY OF AGRICULTURAL SCIENCES   (India)

Author keywords

Acceleration; Barstar; GroEL; Refolding kinetics; Thermodynamic coupling

Indexed keywords

CHAPERONIN;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 0034646559     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3648     Document Type: Article

References (40)

1. Initial hydrophobic collapse in the folding of barstar
2. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
3. On-pathway versus off-pathway folding intermediates
4. Observation of multistate kinetics during the slow folding and unfolding of barstar
5. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
6. GroE facilitates refolding of citrate synthase by suppressing aggregation
7. Purification of GroEL with low fluorescence background
8. The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding
9. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
10. In vivo observation of polypeptide flux through the bacterial chaperonin system
11. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes
12. GroEL-mediated protein folding
13. Residues in chaperonin GroEL required for polypeptide binding and release
14. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
15. Refolding of barnase in the presence of GroE
16. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
17. Effect of GroEL on the re-folding kinetics of α-lactalbumin
18. In vitro dissociation and self-assembly of three chaperonin 60s: The role of ATP
19. Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate
20. Folding of tryptophan mutants of barstar: Evidence for an initial hydrophobic collapse on the folding pathway
21. Submilli-second events in protein folding
22. Circular dichroism of denatured barstar suggests residual structure
23. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
24. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
25. The refolding of cis- and trans-peptidylpropyl isomers of barstar
26. The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates
27. Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone
28. Chaperonin function: Folding by forced unfolding
29. Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
30. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
31. Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
32. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
33. + dependent
34. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
35. A thermodynamic coupling mechanism for GroEL-mediated unfolding
36. GroEL-mediated protein folding proceeds by multiple rounds of binding and release
37. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase
38. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
39. Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
40. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB