How fast is protein hydrophobic collapse?

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

Volumn 100, Issue 21, 2003, Pages 12117-12122

  Sadqi, Mourad ^a   Lapidus, Lisa J ^b,c   Muñoz, Victor ^a  

^a University of Maryland   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

ARTICLE; ENERGY TRANSFER; FLUORESCENCE; GLASS TRANSITION TEMPERATURE; HIGH TEMPERATURE PROCEDURES; LASER; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

BIOPHYSICS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KETOGLUTARATE DEHYDROGENASE COMPLEX; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; THERMODYNAMICS;

EID: 0142059837     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2033863100     Document Type: Article

References (44)

1. Baldwin, R. L. (2002) Science 295, 1657-1658.
2. Williams, S., Causgrove, T. P., Gilmanshin, R., Fang, K. S., Callender, R. H., Woodruff, W. H., & Dyer, R. B. (1996) Biochemistry 35, 691-697.
3. Muñoz, V., Thompson, P. A., Hofrichter, J. & Eaton, W. A. (1997) Nature 390, 196-199.
4. de Gennes, P. G. (1985) J. Phys. Lett. 46, L639-L642.
5. Grosberg, A. Y., Nechaev, S. K. & Shakhnovich, E. I. (1988) J. Phys. 49, 2095-2100.
6. Pitard, E. & Orland, H. (1998) Europhys. Lett. 41, 467-472.
7. Kutnetsov, Y. A., Timoschenko, E. G. & Dawson, K. A. (1995) J. Chem. Phys. 103, 3338-3347.
8. Bryngelson, J. D. & Wolynes, P. G. (1987) Proc. Natl. Acad. Sci. USA 84, 7524-7528.
9. Camacho, C. J. & Thirumalai, D. (1993) Proc. Natl. Acad. Sci. USA 90, 6369-6372.
10. Gutin, A. M., Abkevich, V. I. & Shakhnovich, E. I. (1995) Biochemistry 34, 3066-3076.
11. Onuchic, J., Luthey-Schulten, Z. & Wolynes, P. G. (1997) Annu. Rev. Phys. Chem. 48, 545-600.
12. Dill, K. A. & Chan, H. S. (1997) Nat. Struct. Biol. 4, 10-19.
13. Dobson, C. M., Sali, A. & Karplus, M. (1998) Angew. Chem. Im. Ed. 37, 868-893.
14. Eaton, W. A., Muñoz, V., Hagen, S. J., Jas, G. S., Lapidus, L. J., Henry, E. R. & Hofrichter, J. (2000) Annu. Rev. Biophys. Biomol. Struct. 29, 327-359.
15. Ballew, R. M., Sabelko, J. & Gruebele, M. (1996) Proc. Natl. Acad. Sci. USA 93, 5759-5764.
16. Sabelko, J., Ervin, J. & Gruebele, M. (1999) Proc. Natl. Sci. USA 96, 6031-6036.
17. Roder, H. & Shastry, M. C. (1999) Curr. Opin. Struct. Biol. 9, 620-626.
18. Hagen, S. J. & Eaton, W. A. (2000) J. Mol. Biol. 301, 1019-1027.
19. Akiyama, S., Takahashi, S., Kimura, T., Ishimori, K., Morishima, I., Nishikawa, Y. & Fujisawa, T. (2002) Proc. Natl. Acad. Sci. USA 99, 1329-1334.
20. Mayor, U., Guydosh, N. R., Johnson, C. M., Grossmann, J. G., Sato, S., Jas, G. S., Freund, S. M., Alonso, D. O., Daggett, V. & Fersht, A. R. (2003) Nature 421, 863-867.
21. Yang, W. Y. & Gruebele, M. (2003) Nature 423, 193-197.
22. Hagen, S. J., Hofrichter, J., Szabo, A. & Eaton, W. A. (1996) Proc. Natl. Acad. Sci. USA 93, 11615-11617.
23. Garcia-Mira, M. M., Sadqi, M., Fisher, N., Sanchez-Ruiz, J. M. & Muñoz, V. (2002) Science 298, 2191-2195.
24. Callender, R. & Dyer, R. B. (2002) Curr. Opin. Struct. Biol. 12, 628-633.
25. Lapidus, L. J., Steinbach, P. J., Eaton, W. A., Szabo, A. & Hofrichter, J. (2002) J. Phys. Chem. B 106, 11628-11640.
26. Robien, M. A., Clore, M., Omichinski, J. G., Perham, R. N., Appella, E., Sakaguchi, K. & Gronenborn, A. M. (1992) Biochemistry 31, 3463-3471.
27. Murphy, K. P., Privalov, P. L. & Gill, S. J. (1990) Science 247, 559-561.
28. Guzman-Casado, M., Parody-Morreale, A., Robic, S., Marqusee, S. & Sanchez-Ruiz, J. M. (2003) J. Mol. Biol. 329, 731-743.
29. Flory, P. J. (1969) Statistical Mechanics of Chain Molecules (Interscience, New York).
30. Thirumalai, D. (1995) J. Phys. I France 5, 1457-1467.
31. Duan, Y. & Kollman, P. A. (1998) Science 282, 740-744.
32. Zagrovic, B., Snow, C. D., Shirts, M. R. & Pande, V. S. (2002) J. Mol. Biol. 323, 927-937.
33. Qiu, L., Zachariah, C. & Hagen, S. J. (2003) Phys. Rev. Lett. 90, 168103.
34. Szabo, A., Schulten, K. & Schulten, Z. J. (1980) J. Chem. Phys. 72, 4350-4357.
35. Bryngelson, J. D., Onuchic, J. N., Socci, N. D. & Wolynes, P. G. (1995) Proteins Struct. Funct. Genet. 21, 167-195.
36. Scalley, M. L. & Baker, D. (1997) Proc. Natl. Acad. Sci. USA 94, 10636-10640.
37. Chahine, J., Nymeyer, H., Leite, V. B., Socci, N. D. & Onuchic, J. N. (2002) Phys. Rev. Lett. 88, 168101.
38. Zwanzig, R. (1988) Proc. Natl. Acad. Sci. USA 85, 2029-2030.
39. Plaxco, K. W., Simons, K. T. & Baker, D. (1998) J. Mol. Biol. 277, 985-994.
40. Gillespie, B. & Plaxco, K. W. (2000) Proc. Natl. Acad. Sci. USA 97, 12014-12019.
41. Millet, I. S., Doniach, S. & Plaxco, K. W. (2002) Adv. Protein Chem. 62, 241-262.
42. Schuler, B., Lipman, E. A. & Eaton, W. A. (2002) Nature 419, 743-747.
43. Muñoz, V. & Serrano, L. (1994) Nat. Struct. Biol. 1, 399-409.
44. Muñoz, V. (2001) Curr. Opin. Struct. Biol. 11, 212-216.