Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 9, 1996, Pages 4030-4035

  Todd, Matthew J ^a   Lorimer, George H ^a   Thirumalai, D ^b  

^a DUPONT COMPANY   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; RIBULOSEBISPHOSPHATE CARBOXYLASE;

ARTICLE; CATALYSIS; COOLING; HEATING; HYDROLYSIS; MODEL; PRIORITY JOURNAL; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATE; CHAPERONINS; GROEL PROTEIN; KINETICS; MODELS, STRUCTURAL; PROTEIN CONFORMATION; PROTEIN FOLDING; RIBULOSE-BISPHOSPHATE CARBOXYLASE; THERMODYNAMICS;

EID: 0030006212     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.9.4030     Document Type: Article

References (46)

1. Anfinsen, C. B. (1973) Science 181, 223-230.
2. Wolynes, P. G., Onuchic, J. N. & Thirumalai, D. (1995) Science 267, 1619-1620.
3. Bryngelson, J. D., Onuchic, J. N., Socci, N. D. & Wolynes, P. G. (1995) Proteins Struct. Funct. Genet. 21, 167-196.
4. Dill, K. A., Bromberg, S., Yue, K., Fiebig, K. M., Yee, D. P., Thomas, P. D. & Chan, H. S. (1995) Protein Sci. 4, 561-602.
5. Schmidt, M., Buchner, J., Todd, M. J., Lorimer, G. H. & Viitanen, P. V. (1994) J. Biol. Chem. 269, 10304-10311.
6. Thirumalai, D. (1994) in Statistical Mechanics, Protein Structure, and Protein-Substrate Interactions, ed. Doniach, S. (Plenum, New York), pp. 115-134.
7. Gulukota, K. & Wolynes, P. G. (1994) Proc. Natl. Acad. Sci. USA 91, 9292-9296.
8. Sfatos, C. D., Gutin, A. M., Abkevich, V. I. & Shakhnovich, E. I. (1996) Biochemistry 35, 334-339.
9. Chan, H. S. & Dill, K. A. (1996) Proteins Struct. Funct. Genet. 24, 345-351.
10. Lorimer, G. H. (1996) FASEB J. 10, 5-9.
11. Todd, M. J., Viitanen, P. V. & Lorimer, G. H. (1994) Science 265, 659-666.
12. Weissmann, J. S., Kashi, Y., Fenton, W. A. & Horwich, A. L. (1994) Cell 78, 693-702.
13. Harrison, S. C. & Durbin, R. (1985) Proc. Natl. Acad. Sci. USA 82, 4028-4030.
14. Go, N. (1983) Annu. Rev. Biophys. Bioeng. 12, 183-210.
15. Wetlaufer D. B. (1973) Proc. Natl. Acad. Sci. USA 70, 697-701.
16. Thirumalai, D. & Guo, Z. (1994) Biopolymers 35, 137-140.
17. Guo, Z. & Thirumalai, D. (1995) Biopolymers 36, 83-102.
18. Radford, S. E., Dobson, C. M. & Evans, P. A. (1992) Nature (London) 358, 302-307.
19. Kuszewski, J., Clore, M. G. & Gronenborn, A. M. (1994) Protein Sci. 3, 1945-1952.
20. Elöve, G., Bhuyan, A. K. & Roder, H. (1994) Biochemistry 33, 6925-6935.
21. Sosnick, T. R., Mayne, L., Hiller, R. & Englander, S. W. (1994) Nat. Struct. Biol. 1, 149-156.
22. Jackson, E. & Fersht, A. (1991) Biochemistry 30, 10428-10435.
23. Schnidler, T., Herrler, M., Marahiel, M. A. & Schmid, F. X. (1995) Nat. Struct. Biol. 2, 663-673.
24. Kiefhaber, T. (1995) Proc. Natl. Acad. Sci. USA 92, 9029-9033.
25. Udkaonkar, J. B. & Baldwin, R. L. (1990) Proc. Natl. Acad. Sci. USA 87, 8197-8201.
26. Thirumalai, D. (1995) J. Phys. (Paris) I 5, 1457-1467.
27. Peralta, D., Hartman, D. J., Hoogenraad, N. J. & HøJ, P. B. (1994) FEBS Lett. 339, 45-49.
28. Mattingly, J. A., Iriate, A. & Martinez-Carrion, M. (1995) J. Biol. Chem. 270, 1138-1148.
29. Kiefhaber, T., Rudolph, R., Kohler, H. H. & Buchner, J. (1991) Bio/Technology 9, 825-829.
30. Jaenicke, R. (1987) Prog. Biophys. Mol. Biol. 49, 117-237.
31. Viitanen, P. V., Gatenby, A. A. & Lorimer, G. H. (1992) Protein Sci. 1, 363-369.
32. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Jochimiak, A., Norwich, A. L. & Sigler, P. B. (1994) Nature (London) 371, 578-586.
33. Lin, Z., Schwarz, F. P. & Eisenstein, E. (1995) J. Biol. Chem. 270, 1011-1014.
34. Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K. & Plückthun, A (1994) Nature (London) 368, 261-265.
35. Robinson, C. V., Gross, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Hartl, F. U., Dobson, C. M. & Radford, S. E. (1994) Nature (London) 372, 646-651.
36. Okazaki, A., Ikura, T., Nikaido, K. & Kuwajima, K. (1994) Nat. Struct. Biol. 1, 439-446.
37. Jackson, G. S., Staniforth, R. A., Halsall, D. J., Holbrook, J. J., Clarke, A. R. & Burston, S. G. (1993) Biochemistry 32, 2554-2563.
38. Todd, M. J., Viitanen, P. V. & Lorimer, G. H. (1993) Biochemistry 32, 8560-8567.
39. Bochkareva, E. S. & Girshovich, A. S. (1994) J. Biol. Chem. 269, 23869-23871.
40. Kovalenko, O., Yifrach, O. & Horovitz, A. (1994) Biochemistry 33, 14974-14978.
41. Kirkpatrick, S., Gelatt, C. D. & Vecchi, M. P. (1983) Science 220, 671-680.
42. Grey, T. E. & Fersht, A. R. (1993) J. Mol. Biol. 232, 1197-1207.
43. Ranson, N. A., Dunster, N. J., Burston, S. G. & Clarke, A. R. (1995) J. Mol. Biol. 249, 581-586.
44. Viitanen, P. V., Donaldson, G. K., Lorimer, G. H., Lubben, T. H. & Gatenby, A. A. (1991) Biochemistry 30, 9716-9723.
45. van Dyk, T., Gatenby, A. A. & La Rossa, R. (1989) Nature (London) 342, 451-453.
46. Gordon, C. L., Sather, S. K., Casjens, S. & King, J. (1994) J. Biol. Chem. 269, 27941-27951.