Folding kinetics of proteins and cold denaturation

Journal of Chemical Physics

Volumn 129, Issue 15, 2008, Pages

  Collet, Olivier ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

KINETIC ENERGY; MONTE CARLO METHODS; PHASE DIAGRAMS;

ACTIVATION BARRIERS; APOLAR SOLUTES; COLD DENATURATIONS; CONFORMATIONAL SPACES; ENERGY OF SOLVATIONS; FOLDING KINETICS; FOLDING TIMES; HIGH-TEMPERATURE; HYDRATION MODELS; LARGE RANGES; LATTICE MODELS; LOW TEMPERATURES; MONTE-CARLO SIMULATIONS; NATIVE STRUCTURES; RANDOM ENERGY MODELS; SOLVENT QUALITIES; TEMPERATURE DEPENDENTS;

PROTEIN FOLDING;

WATER;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COLD; KINETICS; MONTE CARLO METHOD; PHASE TRANSITION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; TIME;

COLD TEMPERATURE; KINETICS; MODELS, MOLECULAR; MONTE CARLO METHOD; PHASE TRANSITION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; TIME FACTORS; WATER;

EID: 54849432970     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.2992556     Document Type: Article

References (36)

1. C. B. Anfinsen, E. Haber, M. Sela, and F. H. White, Proc. Natl. Acad. Sci. U.S.A. 0027-8424 10.1073/pnas.47.9.1309 47, 1309 (1961).
2. J. D. Bryngelson and P. G. Wolynes, Proc. Natl. Acad. Sci. U.S.A. 0027-8424 10.1073/pnas.84.21.7524 84, 7524 (1987).
3. E. I. Shakhnovich and A. M. Gutin, Nature (London) 0028-0836 10.1038/346773a0 346, 773 (1990).
4. A. Dinner, A. Šali, M. Karplus, and E. Shakhnovich, J. Chem. Phys. 0021-9606 10.1063/1.467769 101, 1444 (1994).
5. E. I. Shakhnovich, Phys. Rev. Lett. 0031-9007 10.1103/PhysRevLett.72.3907 72, 3907 (1994).
6. A. M. Gutin, V. I. Abkevich, and E. I. Shakhnovich, Proc. Natl. Acad. Sci. U.S.A. 92, 1282 (1995). 0027-8424
7. R. Kumar, A. Prabhu, D. Rao, and A. Bhuyan, J. Mol. Biol. 364, 483 (2006). 0022-2836
8. A. Pastore, S. Martin, A. Politou, T. Kondapalli, K. C. Stemmler, and P. Temussi, J. Am. Chem. Soc. 0002-7863 10.1021/ja0714538 129, 5374 (2007).
9. H. Hadi-Alijanvand, F. Ahmad, and A. Moosavi-Movahedi, Protein Journal 26, 395 (2007).
10. S. Whitten, A. Kurtz, M. Pometun, A. Wand, and V. Hilser, Biochemistry 0006-2960 10.1021/bi060855+ 45, 10163 (2007).
11. P. L. Privalov and G. I. Makhatadze, J. Mol. Biol. 0022-2836 10.1016/0022-2836(89)90318-5 205, 737 (1989).
12. W. Kauzmann, Adv. Protein Chem. 0065-3233 10.1016/S0065-3233(08)60608-7 14, 1 (1959).
13. A. Warshel and S. Lifson, J. Chem. Phys. 0021-9606 10.1063/1.1674031 53, 582 (1970).
14. K. Dill, Biochemistry 0006-2960 10.1021/bi00483a001 29, 7133 (1990).
15. S. Premilat and O. Collet, Europhys. Lett. 0295-5075 10.1209/epl/i1997- 00397-8 39, 575 (1997).
16. O. Collet and S. Premilat, J. Mol. Struct.: THEOCHEM 0166-1280 10.1016/0166-1280(95)04433-7 363, 151 (1996).
17. H. Frauenfelder, P. Fenimore, G. Chen, and B. McMahon, Proc. Natl. Acad. Sci. U.S.A. 103, 15469 (2006). 0027-8424
18. O. Collet, Europhys. Lett. 0295-5075 10.1209/epl/i2001-00128-3 53, 93 (2001).
19. O. Collet, Europhys. Lett. 72, 301 (2005). 0295-5075
20. K. A. T. Silverstein, A. D. J. Haymet, and K. A. Dill, J. Chem. Phys. 0021-9606 10.1063/1.480133 111, 8000 (1999).
21. A. Hansen, M. H. Jensen, K. Sneppen, and G. Zocchi, e-print arXiv:cond-mat/9905357.
22. P. De Los Rios and G. Caldarelli, Phys. Rev. E 1063-651X 10.1103/PhysRevE.62.8449 62, 8449 (2000).
23. D. Roccatano, A. Di Nola, and A. Amadei, J. Phys. Chem. B 108, 5756 (2004). 1520-6106
24. C. F. Lopez, R. K. Darst, and P. J. Rossky, J. Phys. Chem. B 112, 5961 (2008). 1520-6106
25. B. A. Patel, P. G. Debenedetti, F. H. Stillinger, and P. J. Rossky, J. Chem. Phys. 0021-9606 10.1063/1.2909974 128, 175102 (2008).
26. C. L. Dias, T. Ala-Nissila, M. Karttunen, I. Vattulainen, and M. Grant, Phys. Rev. Lett. 0031-9007 10.1103/PhysRevLett.100.118101 100, 118101 (2008).
27. N. Metropolis, A. W. Rosenbluth, M. N. Rosenbluth, A. H. Teller, and E. Teller, J. Chem. Phys. 0021-9606 10.1063/1.1699114 21, 1087 (1953).
28. H. S. Chan and K. A. Dill, J. Chem. Phys. 0021-9606 10.1063/1.466677 100, 9238 (1994).
29. A. Ben-Nam, J. Chem. Phys. 0021-9606 10.1063/1.1675414 54, 3682 (1970).
30. N. Muller, Acc. Chem. Res. 0001-4842 10.1021/ar00169a005 23, 23 (1990).
31. B. Lee and G. Graziano, J. Am. Chem. Soc. 0002-7863 10.1021/ja9538389 118, 5163 (1996).
32. R. Baldwin, Proc. Natl. Acad. Sci. U.S.A. 0027-8424 10.1073/pnas.83.21. 8069 83, 8069 (1986).
33. A. Šali, E. Shakhnovich, and M. Karplus, J. Mol. Biol. 0022-2836 10.1006/jmbi.1994.1110 235, 1614 (1994).
34. O. Collet, Phys. Rev. E 1063-651X 10.1103/PhysRevE.67.061912 67, 061912 (2003).
35. M. Cieplak, M. Henkel, J. Karbowski, and J. Banavar, Phys. Rev. Lett. 0031-9007 10.1103/PhysRevLett.80.3654 80, 3654 (1998).
36. J. Onuchic, D. Socci, Z. Luthey-Schulten, and P. Wolynes, Folding Des. 1359-0278 10.1016/S1359-0278(96)00060-0 1, 441 (1996).