Relationship of Leffler (Brønsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates

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

Volumn 101, Issue 40, 2004, Pages 14338-14342

  Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Framework; Hammond; Linear free energy relationships; Marcus; Nucleation condensation

Indexed keywords

ARTICLE; CHEMICAL REACTION; ENERGY; MATHEMATICAL ANALYSIS; PRIORITY JOURNAL; PROTEIN FOLDING; ANIMAL; CHEMICAL MODEL; CHEMISTRY; GENETICS; IN VITRO STUDY; MUTATION; THERMODYNAMICS;

CHYMOTRYPSIN INHIBITOR 2; PEPTIDE; VEGETABLE PROTEIN;

ANIMALS; MODELS, CHEMICAL; MUTATION; PEPTIDES; PLANT PROTEINS; PROTEIN FOLDING; THERMODYNAMICS;

EID: 5144225084     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0406091101     Document Type: Article

References (54)

1. Leffler, J. E. (1953) Science 117, 340-341.
2. Leffler, J. E. & Grunwald, E. (1963) Rates and Equilibria of Organic Reactions (Wiley, New York).
3. Wurthwein, E. U., Lang, G., Schappele, L. H. & Mayr, H. (2002) J. Am. Chem. Soc. 124, 4084-4092.
4. Fersht, A. R., Leatherbarrow, R. J. & Wells, T. N. C. (1986) Nature 322, 284-286.
5. Fersht, A. R., Leatherbarrow, R. & Wells, T. N. C. (1987) Biochemistry 26, 6030-6038.
6. Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995) J. Mol. Biol. 254, 260-288.
7. Matouschek, A. & Fersht, A. R. (1993) Proc. Natl. Acad. Sci. USA 90, 7814-7818.
8. Matouschek, A., Otzen, D. E., Itzhaki, L. S., Jackson, S. E. & Fersht, A. R. (1995) Biochemistry 34, 13656-13662.
9. Oliveberg, M. (2001) Curr. Opin. Struct. Biol. 11, 94-100.
10. Hedberg, L. & Oliveberg, M. (2004) Proc. Natl. Acad. Sci. USA 101, 7606-7611.
11. Hammond, G. S. (1955) J. Am. Chem. Soc. 77, 334-338.
12. Matthews, J. M. & Fersht, A. R. (1995) Biochemistry 34, 6805-6814.
13. Jencks, W. P. (1985) Chem. Rev. 85, 511-527.
14. Matouschek, A., Kellis, J. T., Jr., Serrano, L. & Fersht, A. R. (1989) Nature 340, 122-126.
15. Fersht, A. R., Matouschek, A. & Serrano, L. (1992) J. Mol. Biol. 224, 771-782.
16. Fersht, A. R. (1995) Curr. Opin. Struct. Biol. 5, 79-84.
17. Fersht, A. R. & Sato, S. (2004) Proc. Natl. Acad. Sci. USA 101, 7976-7981.
18. Vendruscolo, M., Paci, E., Dobson, C. M. & Karplus, M. (2001) Nature 409, 641-645.
19. Paci, E., Vendruscolo, M., Dobson, C. M. & Karplus, M. (2002) J. Mol. Biol. 324, 151-163.
20. Li, A. J. & Daggett, V. (1996) J. Mol. Biol. 257, 412-429.
21. Fersht, A. R. & Daggett, V. (2002) Cell 108, 573-582.
22. Fersht, A. R. (2000) Proc. Natl. Acad. Sci. USA 97, 1525-1529.
23. Daggett, V. & Fersht, A. (2003) Nat. Rev. Mol. Cell Biol. 4, 497-502.
24. Lindorff-Larsen, K., Vendruscolo, M., Paci, E. & Dobson, C. M. (2004) Nat. Struct. Mol. Biol. 11, 443-449.
25. Milla, M. E., Brown, B. M., Waldburger, C. D. & Sauer, R. T. (1995) Biochemistry 34, 13914-13919.
26. Fulton, K. F., Main, E. R. G., Daggett, V. & Jackson, S. E. (1999) J. Mol. Biol. 291, 445-461.
27. Cota, E., Steward, A., Fowler, S. B. & Clarke, J. (2001) J. Mol. Biol. 305, 1185-1194.
28. Sato, S., Religa, T. L., Daggett, V. & Fersht, A. R. (2004) Proc. Natl. Acad. Sci. USA 101, 6952-6956.
29. Sanchez, I. E. & Kiefhaber, T. (2003) J. Mol. Biol. 334, 1077-1085.
30. Marcus, R. A. (1968) J. Phys. Chem. 72, 891-899.
31. Shaik, S. S., Schlegel, H. B. & Wolfe, S. (1992) Theoretical Aspects of Physical Organic Chemistry: The Sn2 Mechanism (Wiley, Hoboken, NJ).
32. Humeres, E., Zucco, C., Nunes, M., Debacher, N. A. & Nunes, R. J. (2002) J. Phys. Org. Chem. 15, 570-575.
33. Aqvist, J. & Warshel, A. (1993) Chem. Rev. 93, 2523-2544.
34. Strajbl, M., Shurki, A. & Warshel, A. (2003) Proc. Natl. Acad. Sci. USA 100, 14834-14839.
35. Miyashita, O., Onuchic, J. N. & Wolynes, P. G. (2003) Proc. Natl. Acad. Sci. USA 100, 12570-12575.
36. Plotkin, S. S., Wang, J. & Wolynes, P. G. (1997) J. Chem. Phys. 106, 2932-2948.
37. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
38. Mirny, L. & Shakhnovich, E. (2001) Annu. Rev. Biophys. Biomol. Struct. 30, 361-396.
39. Onuchic, J. N. & Wolynes, P. G. (2004) Curr. Opin. Struct. Biol. 14, 70-75.
40. Ferguson, N., Pires, J. R., Toepert, F., Johnson, C. M., Pan, Y. P., Volkmer-Engert, R., Schneider-Mergener, J., Daggett, V., Oschkinat, H. & Fersht, A. (2001) Proc. Natl. Acad. Sci. USA 98, 13008-13013.
41. Deechongkit, S., Nguyen, H., Powers, E. T., Dawson, P. E., Gruebele, M. & Kelly, J. W. (2004) Nature 430, 101-105.
42. Daggett, V. & Fersht, A. R. (2003) Trends Biochem. Sci. 28, 18-25.
43. Gianni, S., Guydosh, N. R., Khan, F., Caldas, T. D., Mayor, U., White, G. W. N., DeMarco, M. L., Daggett, V. & Fersht, A. R. (2003) Proc. Natl. Acad. Sci. USA 100, 13286-13291.
44. Karplus, M. & Weaver, D. C. (1976) Nature 260, 404-406.
45. Kim, P. S. & Baldwin, R. L. (1982) Annu. Rev. Biochem. 51, 459-489.
46. Ptitsyn, O. B. (1987) J. Protein Chem. 6, 273-293.
47. Jackson, S. E. & Fersht, A. R. (1991) Biochemistry 30, 10428-10435.
48. Oliveberg, M., Tan, Y. J., Silow, M. & Fersht, A. R. (1998) J. Mol. Biol. 277, 933-943.
49. Tan, Y. J., Oliveberg, M. & Fersht, A. R. (1996) J. Mol. Biol. 264, 377-389.
50. Mayor, U., Guydosh, N. R., Johnson, C. M., Grossmann, J. G., Sato, S., Jas, G. S., Freund, S. M. V., Alonso, D. O. V., Daggett, V. & Fersht, A. R. (2003) Nature 421, 863-867.
51. Jackson, S. E. (1998) Folding Des. 3, R81-R91.
52. Garcia-Mira, M. M., Boehringer, D. & Schmid, F. X. (2004) J. Mol. Biol. 339, 555-569.
53. Daggett, V. (2002) Acc. Chem. Res. 35, 422-429.
54. Day, R., Bennion, B. J., Ham, S. & Daggett, V. (2002) J. Mol. Biol. 322, 189-203.