Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant

Protein Science

Volumn 9, Issue 11, 2000, Pages 2109-2117

  Guidry, Jesse J ^a   Moczygemba, Charmaine K ^a   Wittung Stafshede, Pernilla ^a   Steede, N Kalaya ^b   Landry, Samuel J ^b  

^a Tulane University   (United States)

^b TULANE UNIVERSITY   (United States)

Author keywords

Chaperonin; Circular dichroism; Fluorescence; Protein folding; Spectroscopy

Indexed keywords

CHAPERONIN; CHEMICAL AGENT; GUANIDINE; MONOMER; OLIGOMER; POLYPEPTIDE; RECOMBINANT PROTEIN; TYROSINE; UREA;

ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CROSS LINKING; DISSOCIATION CONSTANT; ENTHALPY; ENTROPY; FLUORESCENCE; HUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ESCHERICHIA COLI;

EID: 0034489321     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.11.2109     Document Type: Article

References (40)

1. Circular dichroism and optical rotatory dispersion of proteins and polypeptides
2. Thermodynamic analysis of unfolding and dissociation in lactose repressor protein
3. The structural stability of the co-chaperonin GroES
4. Equilibrium dissociation and unfolding of the Arc repressor dimer
5. The crystal structure of the bacterial chaperonin GroEL at 2.8 A
6. Release of both native and non-native proteins from a cis-only GroEL ternary complex
7. Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
8. The meaning of hydrophobicity
9. Denatured states of proteins
10. The price of lost freedom: Entropy of bimolecular complex formation
11. Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures. Implications for its diverse biological activities
12. Modular structure of transcription factors: Implications for gene regulation
13. Protein folding in the cell
14. Molecular chaperones in cellular protein folding
15. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
16. The crystal structure of the GroES co-chaperonin at 2.8 A resolution
17. How do small single-domain proteins fold?
18. Conserved sequence motifs in bacterial and bacteriophage chaperonins
19. Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10
20. Protein interactions with urea and guanidinium chloride. A calorimetric study
21. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
22. Chemical synthesis of 10 kDa chaperonin. Biological activity suggests chaperonins do not require other molecular chaperones
23. Entropy in biological binding processes: Estimation of translational entropy loss
24. Unfolding thermodynamics of the tetrameric chaperone, SecB
25. Thermodynamics of protein folding
26. Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: A differential scanning calorimetry study
27. Glutaraldehyde as a protein cross-linkage reagent
28. The ins and outs of a molecular chaperone machine
29. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
30. Selective binding and solvent denaturation
31. On the role of groES in the chaperonin-assisted folding reaction. Three case studies
32. Reversible oligomerization and denaturation of the chaperonin GroES
33. Chaperonin function: Folding by forced unfolding
34. Guanidine hydrochloride unfolding of peptide helices: Separation of denaturant and salt effects
35. Preparation of recombinant human Hsp 10
36. Assay of chaperonin-assisted refolding of citrate synthase
37. Renaturation of citrate synthase: Influence of denaturant and folding assistants
38. Monomerheptamer equilibrium of the Escherichia coil chaperonin GroES