A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding

Biochemistry

Volumn 38, Issue 38, 1999, Pages 12460-12470

  Bieri, Oliver ^a   Wildegger, Gudrun ^a   Bachmann, Annett ^a   Wagner, Clemens ^a   Kiefhaber, Thomas ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; SODIUM CHLORIDE;

ARTICLE; ENZYME STRUCTURE; IONIC STRENGTH; KINETICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE;

ANIMALS; CHICKENS; ENZYME STABILITY; KINETICS; MODELS, CHEMICAL; MURAMIDASE; OSMOLAR CONCENTRATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SODIUM CHLORIDE; THERMODYNAMICS; TIME FACTORS;

EID: 0033592403     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9909703     Document Type: Article

References (52)

1. Kim, P. S., and Baldwin, R. L. (1990) Annu. Rev. Biochem. 59, 631-660.
2. Bryngelson, J. D., and Wolynes, P. G. (1989) J. Phys. Chem. 93, 6902-6915.
3. Thirumalai, D. (1994) in Statistical Mechanics, Protein Structure, and Protein Substrate Interactions (Doniach, S., Ed.) pp 115-134, Plenum Press.
4. Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (1995) Proteins: Struct., Funct., Genet. 21, 167-195.
5. Jackson, S. E., and Fersht, A. R. (1991) Biochemistry 30, 10428-35.
6. Alexander, P., Orban, J., and Bryan, P. (1992) Biochemistry 31, 7243-7248.
7. Viguera, A. R., Martínez, J. C., Filimonov, V. V., Mateo, P. L., and Serrano, L. (1994) Biochemistry 33, 2142.
8. Villegas, V., Azuga, A., Catasús, L., Reverter, D., Mateo, P., Avilés, F., and Serrano, L. (1995) Biochemistry 34, 15105-15110.
9. Kragelgund, B. B., Robinson, C. V., Knudsen, J., and Dobson, C. M. (1995) Biochemistry 34, 7117-7224.
10. Schindler, T., Herrler, M., Marahiel, M. A., and Schmid, F. X. (1995) Nat. Struct. Biol. 2, 663-673.
11. Schönbrunner, N., Koller, K.-P., and Kiefhaber, T. (1997) J. Mol. Biol. 268, 526-538.
12. Jonsson, T., Waldburger, C. D., and Sauer, R. T. (1996) Biochemistry 35, 4795-4802.
13. Walkenhorst, W. F., Green, S., and Roder, H. (1997) Biochemistry 36, 5795-5805.
14. Oliveberg, M., Tan, Y.-J., Silow, M., and Fersht, A. R. (1998) J. Mol. Biol. 277, 933-943.
15. Wolynes, P. G. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 6170-6175.
16. Portman, J. J., Takada, S., and Wolynes, P. G. (1998) Phys. Rev. Lett. 81, 5237-5240.
17. Kuwajima, K., Hiraoka, Y., Ikeguchui, M., and Sugai, S. (1985) Biochemistry 24, 874-881.
18. Chaffotte, A. F., Guillou, Y., and Goldberg, M. E. (1992) Biochemistry 31, 9694-9702.
19. Radford, S. E., Dobson, C. M., and Evans, P. A. (1992) Nature 358, 302-307.
20. Segel, D., Bachmann, A., Hofrichter, J., Hodgson, K., Doniach, S., and Kiefhaber, T. (1999) J. Mol. Biol. 288, 489-500.
21. Kiefhaber, T. (1995) Proc. Natl. Acd. Sci. U.S.A. 92, 9029-9033.
22. Wildegger, G., and Kiefhaber, T. (1997) J. Mol. Biol. 271, 294-304.
23. Kiefhaber, T., Bachmann, A., Wildegger, G., and Wagner, C. (1997) Biochemistry, 5108-5112.
24. Kulkarni, S. K., Ashcroft, A. E., Carey, M., Masselos, D., Robinson, C. V., and Radford, S. E. (1999) Protein Sci. 8, 35-44.
25. Mantagne, A., Radford, S. E., and Dobson, C. M. (1997) J. Mol. Biol. 267, 1068-1074.
26. Lewith, S. (1888) Arch. Exp. Pathol. Pharmakol. 24, 1-16.
27. Hofmeister, F. (1888) Arch. Exp. Pathol. Pharmakol. 24, 247-260.
28. von Hippel, P. H., and Wong, K.-Y. (1965) J. Biol. Chem. 240, 3909-3923.
29. Baldwin, R. L. (1996) Biophys. J. 71, 2056-2063.
30. Matsen, F. A., and Franklin, J. L. (1950) J. Am. Chem. Soc. 53, 3337-3341.
31. Segawa, S., and Sugihara, M. (1984) Biopolymers 23, 2437-2488.
32. Schmid, F. X. (1986) Methods Enzymol. 131, 70-82.
33. Hill, T. L. (1974) Prog. Biophys. Mol. Biol. 28, 267-340.
34. Hill, T. L. (1977) Free Energy Transduction in Biology., Academic Press, London.
35. Szabo, Z. G. (1969) in Comprehensive chemical kinetics (Bamford, C. H., and Tipper, C. F. H., Eds.) pp 1-80, Elsevier Publishing Company, Amsterdam.
36. Moore, J. W., and Pearson, R. G. (1981) Kinetics and Mechanisms., John Wiley & Sons, New York.
37. Goto, Y., Calciano, L. J., and Fink, A. L. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 573-577.
38. Goto, Y., Takahashi, N., and Fink, A. L. (1990) Biochemistry 29, 3480-3488.
39. Goto, Y., and Nishikiori, S. (1991) J. Mol. Biol. 222, 679-686.
40. Tanford, C., and Roxby, R. (1972) Biochemistry 11, 2192-2198.
41. Behlke, J., and Ristau, O. (1999) Biophys. Chem. 76, 13-23.
42. Itzhaki, L. S., Evans, P. A., Dobson, C. M., and Radford, S. E. (1994) Biochemistry 33, 5212-5220.
43. Imoto, T., Forster, L. S., Rupley, J. A., and Tanaka, F. (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 1151-1155.
44. Rothwarf, D. M., and Scheraga, H. A. (1996) Biochemistry 35, 13797-13807.
45. Miranker, A. D., Robinson, C. V., Radford, S. E., Aplin, R. T., and Dobson, C. M. (1993) Science 262, 896-900.
46. Radford, S. E., Buck, M., Topping, K. D., Dobson, C. M., and Evans, P. A. (1992) Proteins 14, 237-48.
47. Khorasanizadeh, S., Peters, I. D., and Roder, H. (1996) Nat. Struct. Biol. 3, 193-205.
48. Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Science 269, 192-197.
49. Chamberlain, A. K., Handel, T. M., and Marqusee, S. (1996) Nat. Struct. Biol. 3, 782-787.
50. Clarke, J., Itzhaki, L. S., and Fersht, A. R. (1997) Trends. Biochem. Sci. 22, 284-287.
51. Englander, S. W. (1998) Trends Biochem. Sci 23.
52. Santoro, M. M., and Bolen, D. W. (1988) Biochemistry 27, 8063-8068.