Smoothing the landscapes of protein folding: Insights from a minimal model

Journal of Chemical Physics

Volumn 109, Issue 4, 1998, Pages 1545-1554

  Betancourt, Marcos R ^a  

^a Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001252660     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.476706     Document Type: Article

References (27)

1. C. B. Anfinsen, E. Haber, M. Sela, and F. H. White, Proc. Natl. Acad. Sci. USA 47, 1309 (1961).
2. C. Levinthal, Mossbauer Spectroscopy in Biological Systems in Proceedings of a Meeting Held at Allerton House, Monticello, Illinois, edited by P. DeBrunner, J. Tsibiris, and E. Munck (University of Illinois Press, Urbana, IL, 1969), pp. 22-24.
3. M. R. Betancourt and J. N. Onuchic, J. Chem. Phys. 103, 773 (1995).
4. E. I. Shakhnovich and A. M. Gutin, Proc. Natl. Acad. Sci. USA 90, 7195 (1993).
5. H. W. Chan and x K. A. Dill, J. Chem. Phys. 100, 9238 (1994).
6. J. Bryngelson and P. G. Wolynes, Proc. Natl. Acad. Sci. USA 84, 7524 (1987).
7. J. Bryngelson and P. G. Wolynes, J. Phys. Chem. 93, 6902 (1989).
8. J. Bryngelson, N. D. Socci, J. N. Onuchic, and P. Wolynes, Proteins: Struct., Funct., Genet. 21, 167 (1995).
9. C. J. Camacho and D. Thirumalai, Proc. Natl. Acad. Sci. USA 90, 6369 (1993).
10. H. S. Chan and K. A. Dill, Macromolecules 22, 4559 (1989).
11. H. S. Chan and K. A. Dill, J. Chem. Phys. 92, 3118 (1990).
12. H. S. Chan and K. A. Dill, Proc. Natl. Acad. Sci. USA 87, 6388 (1990).
13. K. F. Lau and K. A. Dill, Macromolecules 22, 3986 (1989).
14. H. S. Chan and K. A. Dill, J. Chem. Phys. 95, 3775 (1991).
15. H. S. Chan and K. A. Dill, Annu. Rev. Biophys. Biophys. Chem. 20, 447 (1991).
16. R. Miller, C. A. Danko, M. J. Fasolka, A. C. Balazs, H. S. Chan, and K. A. Dill, J. Chem. Phys. 96, 768 (1992).
17. J. N. Onuchic, P. G. Wolynes, Z. A. Luthey-Schulten, and N. D. Socci, Proc. Natl. Acad. Sci. USA 92, 3626 (1995).
18. N. Metropolis, A. W. Rosenbluth, M. N. Rosenbluth, and A. H. Teller, J. Chem. Phys. 21, 1087 (1953).
19. H. Verdier and W. H. Stockmayer, J. Chem. Phys. 36, 227 (1962).
20. P. H. Verdier, J. Chem. Phys. 59, 6119 (1973).
21. H. Taketomi, Y. Ueda, and N. Go, Int. J. Pept. Protein Res. 7, 445 (1975).
22. P. Leopold, M. Montal, and N. Onuchic, Proc. Natl. Acad. Sci. USA 89, 8721 (1992).
23. N. D. Socci and J. N. Onuchic, J. Chem. Phys. 101, 1519 (1994).
24. J. Skolnick and A. Kolinski, J. Mol. Biol. 212, 787 (1989).
25. C. J. Camacho and D. Thirumalai, Proc. Natl. Acad. Sci. USA 90, 2146 (1993).
26. Notice that moving a group of residues (r
27. It is easy to see that for r