Thermodynamics of transient conformations in the folding pathway of barnase: Reorganization of the folding intermediate at low pH

Biochemistry

Volumn 35, Issue 8, 1996, Pages 2738-2749

  Oliveberg, Mikael ^a   Fersht, Alan R ^a  

^a MRC CENTRE FOR PROTEIN ENGINEERING   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BARNASE; RIBONUCLEASE; UNCLASSIFIED DRUG;

ARTICLE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMODYNAMICS;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTONS; RIBONUCLEASES; SODIUM CHLORIDE; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 0029988634     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi950967t     Document Type: Article

References (49)

1. Arcus, V., Vuilleumier, S., Freund, S. M. V., Bycroft, M., & Fersht, A. R. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 9412-9416.
2. Arcus, V. L., Vuilleumier, S. V., Freund, S. M. V., Bycroft, M., & Fersht, A. R. (1995) J. Mol. Biol. 254, 305-321.
3. Barrick, D., & Baldwin, R. L. (1993) Protein Sci. 2, 869-876.
4. Briggs, M. S., & Roder, H. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2017-2021.
5. Chaffotte, A. F., Guillou, Y., & Goldberg, M. E. (1992) Biochemistry 31, 9694-9702.
6. Chen, B., Baase, W. A., & Schellman, J. A. (1989) Biochemistry 26, 691-699.
7. Creighton, T. E. (1992) In Protein Folding (Creighton, T. E., Ed.) pp 301-351, W. H. Freeman and Co., New York.
8. Dill, K. A., & Shortle, D. (1991) Annu. Rev. Biochem. 60, 795-825.
9. Dobson, C. M. (1992) Curr. Opin. Struct. Biol. 2, 6-12.
10. Griko, Y. V., Freire, E., & Privalov, P. I. (1994a) Biochemistry 33, 1889-1899.
11. Griko, Y. V., Makhatadze, G. I., Privalov, P. L., & Hartley, R. W. (1994b) Protein Sci. 3, 669-676.
12. Hendsch, Z. S., & Tidor, B. (1994) Protein Sci. 3, 211-226.
13. Jennings, P. A., & Wright, P. E. (1993) Science 262, 892-896.
14. Kiefhaber, T., & Schmid, F. X. (1992) J. Mol. Biol. 224, 231-240.
15. Kiefhaber, T., Kohler, H.-H., & Schmid, F. X. (1992) J. Mol. Biol. 224, 211-239.
16. Kim, P. S., & Baldwin, R. L. (1990) Annu. Rev. Biochem. 59, 631-660.
17. Kuwajima, K. (1989) Proteins: Struct., Funct., Genet. 6, 87-103.
18. Kuwajima, K., Hiraoka, Y., Ikeguchi, M., & Sugai, S. (1985) Biochemistry 24, 874-881.
19. Kuwajima, K., Gravey, E. P., Finn, B. E., Matthews, C. R., & Sugai, S. (1991) Biochemistry 10, 7693-7703.
20. Lu, J., & Dahlquist, F. W. (1992) Biochemistry 31, 4749-4756.
21. Makhatadze, G. I., & Privalov, P. L. (1990) J. Mol. Biol. 213, 375-384.
22. Martinez, J. C., El Harrous, M., Filimonov, V. V., Mateo, P. L., & Fersht, A. R. (1994) Biochemistry 33, 3919-3926.
23. Matouschek, A., Kellis, J. T., Jr., Serrano, L., & Fersht, A. R. (1989) Nature 342, 122-126.
24. Matouschek, A., Kellis, J. T., Jr., Serrano, L., Bycroft, M., & Fersht, A. R. (1990) Nature 346, 440-445.
25. Matouschek, A., Serrano, L., & Fersht, A. R. (1992) J. Mol. Biol. 224, 819-835.
26. Nishii, I., Kataoka, M., Tokunaga, F., & Goto, Y. (1994) Biochemistry 33, 4903-4909.
27. Oliveberg, M., & Fersht, A. R. (1996) Biochemistry 35, 2726-2737.
28. Oliveberg, M., Vuilleumier, S., & Fersht, A. R. (1994) Biochemistry 33, 8826-8832.
29. Oliveberg, M., Tan, Y.-J., & Fersht, A. R. (1995a) Proc. Natl. Acad. Sci. U.S.A. 92, 8926-8929.
30. Oliveberg, M., Arcus, V., & Fersht, A. R. (1995b) Biochemistry 34, 9424-9433.
31. Privalov, P. L. (1992) In Protein Folding (Creighton, T. E., Ed.) pp 83-126, W. H. Freeman and Co., New York.
32. Privalov, P. L., & Gill, S. J. (1988) Adv. Protein Chem. 39, 191-234.
33. Privalov, P. L., & Makhatadze, G. I. (1990) J. Mol. Biol. 213, 385-391.
34. Privalov, P. L., Griko, Y. V., Venyaminov, S. Y., & Kutyshenko, V. P. (1986) J. Mol. Biol. 190, 487-498.
35. Privalov, P. L., Tiktopulo, E. I., Venyaminov, S. Y., Griko, Y. V., Makhatadze, G. I., & Khechinashvili, N. N. (1989) J. Mol. Biol. 205, 737-750.
36. Ptitsyn, O. B. (1992) in Protein Folding (Creighton, T. E., Ed.) W. H. Freeman and Co., New York.
37. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., & Razgulyaev, O. I. (1990) FEBS Lett. 12, 20-24.
38. Radford, S. E., Dobson, C. M., & Evans, P. A. (1992) Nature 358, 302-307.
39. Roder, H., Elöve, G. A., & Englander, S. W. (1988) Nature 335, 694-699.
40. Schmid, F. X., & Baldwin, R. L. (1979) J. Mol. Biol. 135, 199-215.
41. Schreiber, G., & Fersht, A. R. (1993) Biochemistry 32, 11195-11203.
42. Semisotnov, G. V., Rodinova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas', A. F., & Gilmanshin, R. I. (1991) Biopolymers 31, 119-128.
43. Serrano, L., Matouschek, A., & Fersht, A. R. (1992) J. Mol. Biol. 224, 805-818.
44. Shakhnovich, E. I., & Finkelstein, A. V. (1989) Biopolymers 28, 1667-1680.
45. Sturtevant, J. M. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 2236-2240.
46. Sugihara, M., & Segawa, S. (1984) Biopolymers 23, 2473.
47. Svensson, M., Jonasson, P., Freskgård, P.-O., Jonsson, B.-H., Lindgren, M., Mårtensson, L.-G., Gentile, M., Borén, K., & Carlsson, U. (1995) Biochemistry 34, 8606-8620.
48. Udgaonkar, J. B., & Baldwin, R. L. (1990) Proc. Natl. Acad. Sci. U.S.A. 57, 8197-8201.
49. Yutani, K., Ogasahara, K., & Kuwajima, K. (1992) J. Mol. Biol. 228, 347-350.