Folding kinetics of villin 14T, a protein domain with a central β- sheet and two hydrophobic cores

Biochemistry

Volumn 37, Issue 41, 1998, Pages 14508-14518

  Choe, Sung E ^a   Matsudaira, Paul T ^b   Osterhout, John ^c   Wagner, Gerhard ^d   Shakhnovich, Eugene I ^e  

^a HARVARD UNIVERSITY   (United States)

^b WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^c HARVARD UNIVERSITY   (United States)

^d HARVARD MEDICAL SCHOOL   (United States)

^e HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANIDINE; HYDROGEN; UREA; VILLIN;

ARTICLE; HYDROGEN BOND; HYDROPHOBICITY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

ANIMALS; CARRIER PROTEINS; CHICKENS; GUANIDINE; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MICROFILAMENT PROTEINS; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THERMODYNAMICS; UREA;

EID: 0032514727     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980889k     Document Type: Article

References (54)

1. Anfinsen, C. B., Haber, E., Sela, M., and White, F. H. (1961) Proc. Natl. Acad. Sci. U.S.A. 47, 1309-1314.
2. Levinthal, C. (1968) J. Chem. Phys. 65, 44-45.
3. Lopez-Hernandez, E., and Serrano, L. (1996) Folding Des. 1, 43-55.
4. Shastry, M. C., and Udgaonkar, J. B. (1995) J. Mol. Biol. 247, 1013-1027.
5. Wildegger, G., and Kiefhaber, T. (1997) J. Mol. Biol. 270, 294-304.
6. Jones, B. E., and Matthews, C. R. (1995) Protein Sci. 4, 167-177.
7. Varley, P., Gronenborn, A. M., Christensen, H., Wingfield, P. T., Pain, R. H., and Clore, G. M. (1993) Science 260, 1110-1113.
8. Udgaonkar, J. B., and Baldwin, R. L. (1988) Nature 335, 694-699.
9. Khorasanizadeh, S., Peters, I. D., and Roder, H. (1996) Nat. Struct. Biol. 3, 193-205.
10. Matouschek, A., Serrano, L., and Fersht, A. R. (1992) J. Mol. Biol. 224, 819-835.
11. Dobson, C. M., Evans, P. A., and Radford, S. E. (1994) Trends Biochem. Sci. 19, 31-37.
12. Weissman, J. S., and Kim, P. S. (1991) Science 253, 1386-1393.
13. Elove, G. A., Bhuyan, A. K., and Roder, H. (1994) Biochemistry 33, 6925-6935.
14. Baldwin, R. L. (1996) Folding Des. 1, R1-R8.
15. Heidary, D. K., Gross, L. A., Roy, M., and Jennings, P. A. (1997) Nat. Struct. Biol. 4, 725-731.
16. Kiefhaber, T. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 9029-9033.
17. Kuszewski, J., Clore, G. M., and Gronenborn, A. M. (1994) Protein Sci. 3, 1945-1952.
18. Alexander, P., Orban, J., and Bryan, P. (1992) Biochemistry 31, 7243-7248.
19. Villegas, V., Azuaga, A., Catasus, L., Reverter, D., Mateo, P. L., Aviles, F. X., and Serrano, L. (1995) Biochemistry 34, 15105-15110.
20. Jackson, S. E., and Fersht, A. R. (1991) Biochemistry 30, 10428-10435.
21. Kragelund, B. B., Robinson, C. V., Knudsen, J., Dobson, C. M., and Poulsen, F. M. (1995) Biochemistry 34, 7217-7224.
22. Huang, G. S., and Oas, T. G. (1995) Biochemistry 34, 3884-3892.
23. Schonbrunner, N., Koller, K. P., and Kiefhaber, T. (1997) J. Mol. Biol. 268, 526-538.
24. Viguera, A. R., Martinez, J. C., Filimonov, V. V., Mateo, P. L., and Serrano, L. (1994) Biochemistry 33, 2142-2150.
25. Jackson, S. E., el Masry, N., and Fersht, A. R. (1993) Biochemistry 32, 11270-11278.
26. Shakhnovich, E., Abkevich, V., and Ptitsyn, O. (1996) Nature 379, 96-98.
27. Khorasanizadeh, S., Peters, I. D., Butt, T. R., and Roder, H. (1993) Biochemistry 32, 7054-7063.
28. Matouschek, A., and Kellis, J. T. (1990) Nature 346, 440-445.
29. Munoz, V., Lopez, E. M., Jager, M., and Serrano, L. (1994) Biochemistry 33, 5858-5866.
30. Creighton, T. E. (1994) Nat. Struct. Biol. 1, 135-138.
31. Sosnick, T. R., Mayne, L., Hiller, R., and Englander, S. W. (1994) Nat. Struct. Biol. 1, 149-156.
32. Sosnick, T. R., Mayne, L., and Englander, S. W. (1996) Proteins: Struct., Funct., Genet. 24, 413-426.
33. Matsudaira, P. T., and Burgess, D. R. (1982) J. Cell Biol. 92, 648-656.
34. Markus, M. A., Nakayama, T., Matsudaira, P., and Wagner, G. (1994) Protein Sci. 3, 70-81.
35. Markus, M. A., Matsudaira, P., and Wagner, G. (1997) Protein Sci. 6, 1197-1209.
36. Doering, D. S., and Matsudaira, P. (1996) Biochemistry 35, 12677-12685.
37. Pace, C. N. (1986) Methods Enzymol. 131, 266-280.
38. Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T., and Dobson, C. M. (1993) Science 262, 896-900.
39. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Protein Sci. 4, 2138-2148.
40. Jackson, S. E., and Fcrsht, A. R. (1991) Biochemistry 30, 10436-10443.
41. Silow, M., and Oliveberg, M. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 6084-6086.
42. Szabo, Z. G. (1969) Comprehensive Chemical Kinetics 2, 24-26.
43. Connelly, G. P., Bai, Y., Jeng, M. F., and Englander, S. W. (1993) Proteins 17, 87-92.
44. Englander, S. W., and Kallenbach, N. R. (1983) Q. Rev. Biophys. 16, 521-655.
45. Sosnick, T. R., Shtilerman, M. D., Mayne, L., and Englander, S. W. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 8545-8550.
46. Cantor, C. R., and Schimmel, P. R. (1980) Biophysical Chemistry, Part 1: The Conformation of Biological Macromolecules, W. H. Freeman and Co., New York.
47. Privalov, P. L., and Gill, S. J. (1988) Adv. Protein Chem. 39, 191-234.
48. Tanford, C. (1980) The Hydrophobic effect: formation of micelles and biological membranes, 2nd ed., Wiley-Interscience, New York.
49. Milla, M. E., Brown, B. M., Waldburger, C. D., and Sauer, R. T. (1995) Biochemistry 34, 13914-13919.
50. Itzhaki, L. S., Otzen, D. E., and Fersht, A. R. (1995) J. Mol. Biol. 254, 260-288.
51. Sosnick, T. R., Jackson, S., Wilk, R. R., Englander, S. W., and Degrado, W. F. (1996) Proteins: Struct., Funct., Genet. 24, 427-432.
52. Mayr, L. M., and Schmid, F. X. (1993) Biochemistry 32, 7994-7998.
53. Monera, O. D., Kay, C. M., and Hodges, R. T. (1994) Protein Sci. 3, 1984-1991.
54. Kraulis, P. (1991) J. Appl. Crystallogr. 24, 946-950.