The structural stability of the co-chaperonin GroES

Journal of Molecular Biology

Volumn 272, Issue 5, 1997, Pages 770-779

  Boudker, Olga ^a   Todd, Matthew J ^a   Freire, Ernesto ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

Calorimetry; Chaperonins; GroES; Protein folding; Thermodynamics

Indexed keywords

CHAPERONIN; GLOBULAR PROTEIN; MAGNESIUM ION; MONOMER; OLIGOMER; PROTEIN SUBUNIT; SODIUM CHLORIDE;

ARTICLE; BINDING SITE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; DISSOCIATION CONSTANT; ESCHERICHIA COLI; MOLECULAR WEIGHT; NONHUMAN; OLIGOMERIZATION; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 0031563834     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1263     Document Type: Article

References (25)

1. Bardi J. S., Luque I., Freire E. Structure-based thermodynamic analysis of HIV-1 protease inhibitors. Biochemistry. 22:1997;6588-6596.
2. Braig K., Otwinowski Z., Hegde R., Boisvert D. C., Joachimiak A., Horwich A. L., Sigler P. B. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature. 371:1994;578-586.
3. DAquino J. A., Gómez J., Hilser V. J., Lee K. H., Amzel L. M., Freire E. The magnitude of the backbone conformational entropy change in protein folding. Proteins: Struct. Funct. Genet. 25:1996;143-156.
4. Freire E. Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions. Comm. Mol. Cell. Biophys. 6:1989;123-140.
5. Golubinoff P., Gatenby A. A., Lorimer G. H. GroE heat-shock proteins promote assembly of forein prokaryotic ribulose bisphosphate carboxylase oligomers inEscherichia coli. Nature. 337:1989;44-47.
6. Gomez J., Freire E. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252:1995;337-350.
7. Gomez J., Hilser J. V., Xie D., Freire E. The heat capacity of proteins. Proteins: Struct. Funct. Genet. 22:1995;404-412.
8. Hilser V. J., Gomez J., Freire E. The enthalpy change in protein folding and binding. refinement of parameters for structure based calculations. Proteins: Struct. Funct. Genet. 26:1996;123-133.
9. Hunt J. F., Weaver A. J., Landry S. J., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
10. Johnson C. R., Freire E. Structural stability of oligomeric proteins. Techn. Prot. Chem. VII:1996;459-467.
11. Johnson C. R., Morin P. E., Arrowsmith C. H., Freire E. Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppresor. Biochemistry. 34:1995;5309-5316.
12. Kenar K. T., García-Moreno B., Freire E. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci. 4:1995;1934-1938.
13. Landry S. J., Zeilstra-Ryalls J., Fayet O., Georgopoulos C., Gierasch L. M. Characterization of a functionally important mobile domain of GroES. Nature. 364:1993;255-258.
14. Landry S. J., Taher A., Georgopoulos C., van der Vies S. M. Interplay of structure and disorder in cochaperonin mobile loops. Proc. Natl Acad. Sci. USA. 93:1996;11622-11627.
15. Luque I., Mayorga O., Freire E. Structure based thermodynamic scale of α-helix propensities in amino acids. Biochemistry. 35:1996;13681-13688.
16. Makhatadze G. I., Privalov P. L. Protein interactions with urea and guanidinium chloride. A calorimetric study. J. Mol. Biol. 226:1992;491-505.
17. Mande S. C., Mehra V., Bloom B. R., Hol W. G. J. Structure of the heat shock protein chaperonin-10 ofMycobacterium leprae. Science. 271:1996;203-207.
18. Seale J. W., Horowitz P. M. The C-terminal sequence of the chaperonin GroES is required for oligomerization. J. Biol. Chem. 270:1995;30268-30270.
19. Seale J. W., Gorovits B. M., Ybarra J., Horowitz P. M. Reversible oligomerization and denaturation of the chaperonin GroES. Biochemistry. 35:1996;4079-4083.
20. Swint-Kruse L., Robertson A. D. Hydrogen bonds and the pH dependence of ovomucoid third domain stability. Biochemistry. 34:1995;4724-4732.
21. Thompson K., Vinson C., Freire E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry. 32:1993;5491-5496.
22. Todd M. J., Viitanen P. V., Lorimer G. H. Hydrolysis of adenosine 5′ triphophate byEsherichia coli. Biochemistry. 32:1993;8560-8567.
23. van der Vies S. M., Viitanen P. V., Gatenby A. A., Lorimer G. H., Jaenicke R. Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. Biochemistry. 31:1992;3635-3644.
24. Weissman J. S., Hohl C. M., Kovalenko O., Kashi Y., Chen S., Braig K., Saibil H. R., Fenton W. A., Horwich A. L. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell. 83:1995;577-587.
25. Zondlo J., Fisher K. E., Lin Z., Ducote K. R., Eisenstein E. Monomer heptamer equilibrium of theEsherichia coli. Biochemistry. 34:1995;10334-10339.