Fast and Slow Folding in Cytochrome c

Accounts of Chemical Research

Volumn 31, Issue 11, 1998, Pages 737-744

  Englander, S Walter ^a,b,c,d   Sosnick, Tobin R ^a,c,e   Mayne, Leland C ^a,c,f,g   Shtilerman, Mark ^a,c,h   Qi, Phoebe X ^a,c,i   Bai, Yawen ^a,c,j,k  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PITTSBURGH   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d NATIONAL ACADEMY OF SCIENCES   (United States)

^e UNIVERSITY OF CHICAGO   (United States)

^f UNIVERSITY OF OREGON   (United States)

^g JOHNSON RESEARCH   (United States)

^h ST PETERSBURG STATE UNIVERSITY   (Russian Federation)

ⁱ UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^j SCRIPPS RESEARCH INSTITUTE   (United States)

^k NATIONAL INSTITUTES OF HEALTH   (United States)

more..

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0000108661     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar970085h     Document Type: Article

References (39)

1. Sosnick, T. R.; Mayne, L.; Englander, S. W. Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins 1996, 24, 413-426.
2. Sosnick, T. R.; Shtilerman, M. D.; Mayne, L.; Englander, S. W. Ultrafast signals in protein folding and the polypeptide contracted state. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 8545-8550.
3. Qi, P. X.; Sosnick, T. R.; Englander, S. W. The burst phase in ribonuclease A folding: Solvent dependence of the unfolded state. Nature Struct. Biol. 1998, 5, 882-884.
4. Roder, H.; Elöve, G. A.; Englander, S. W. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 1988, 335, 700-704.
5. Bai, Y.; Sosnick, T. R.; Mayne, L.; Englander, S. W. Protein folding intermediates studied by native state hydrogen exchange. Science 1995, 269, 192-197.
6. Sosnick, T. R.; Mayne, L.; Hiller, R.; Englander, S. W. The barriers in protein folding. Nature Struct. Biol. 1994, 1, 149-156.
7. Brems, D. N.; Stellwagen, E. Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c. J. Biol. Chem. 1983, 258, 3655-3660.
8. Kuroda, Y. Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry 1993, 32, 1219-1224.
9. Robertson, A. D.; Baldwin, R. L. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry 1991, 30, 9907-14.
10. Ikai, A.; Fish, W. W.; Tanford, C. Kinetics of unfolding and refolding of proteins. II Results for cytochrome c. J. Mol. Biol. 1973, 73, 165-184.
11. Jackson, S. E.; Fersht, A. R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 1991, 30, 10428-10435.
12. Chen, X.; Matthews, C. R. Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry 1994, 33, 6356-62.
13. Bryngelson, J. D.; Onuchic, J. N.; Socci, N. D.; Wolynes, P. G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 1995, 21, 167-95.
14. Dill, K. A.; Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 1997, 4, 10-19.
15. Abkevich, V. I.; Gutin, A. M.; Shakhnovich, E. I. Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry 1994, 33, 10026-36.
16. Thirumalai, D.; Guo, Z. Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange experiments. Biopolymers 1995, 35, 137-140.
17. Fersht, A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 10869-73.
18. Fersht, A. R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 1997, 7, 3-9.
19. Makhatadze, G. I.; Privalov, P. L. Protein interactions with urea and guanidinium chloride. A calorimetric study. J. Mol. Biol. 1992, 226, 491-505.
20. Xie, D.; Fox, R.; Freire, E. Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. Protein Sci. 1994, 3, 2175-84.
21. Ptitsyn, O. B. Kinetic and equilibrium intermediates in protein folding. Protein Eng. 1994, 7, 593-596.
22. Creighton, T. E. The energetic ups and downs of protein folding. Nature Struct. Biol. 1994, 1, 135-138.
23. Ptitsyn, O. B. Molten globule and protein folding. Adv. Protein Chem. 1995, 47, 83-229.
24. Matthews, C. R. Pathways of protein folding. Annu. Rev. Biochem. 1993, 62, 653-83.
25. Tsong, T. Y.; Baldwin, R. L.; McPhie, P. A sequential model of nucleation dependent protein folding. Kinetic studies of ribonuclease A. J. Mol. Biol. 1972, 63, 453-475.
26. Wetlaufer, D. B. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. U.S.A. 1973, 70, 697-701.
27. Sosnick, T. R.; Englander, S. W. What limits protein folding? In Dynamics and the problem of recognition in biological macromolecules; Jardetzky, O., Lefevre, J.-F., Eds.; Plenum Press: New York, 1996; Vol. 288; pp 65-71.
28. Elöve, G. A.; Bhuyan, A. K.; Roder, H. Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry 1994, 33, 6925-6935.
29. Baldwin, R. L. The nature of protein folding pathways: The classical versus the new view. J. Biomol. NMR 1995, 5, 103-109.
30. Rose, G. D. Hierarchic organization of domains in globular proteins. J. Mol. Biol. 1979, 134, 447-70.
31. Bai, Y.; Englander, S. W. Future directions in folding: the multi-state nature of protein structure. Proteins 1996, 24, 145-51.
32. Chamberlain, A. K.; Handel, T. M.; Marqusee, S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNase H. Nature Struct. Biol. 1996, 3, 782-787.
33. Hiller, R.; Zhou, Z. H.; Adams, M. W. W.; Englander, S. W. Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 °C. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 11329-11332.
34. 562 examined by hydrogen exchange. Biochemistry 1998, 37, 3687-98.
35. 562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 1998, 37, 3687-3698.
36. Fersht, A. R.; Matouschek, A.; Serrano, L. Folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 1992, 224, 771-782.
37. Kraulis, P. J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991, 24, 946-950.
38. Englander, S. W.; Mayne, L. C.; Bai, Y.; Sosnick, T. R. Hydrogen exchange: the modern legacy of Linderstrom-Lang. Protein Sci. 1997, 6, 1101-1109.
39. Houry, W. A.; Rothwarf, D. M.; Scheraga, H. A. Circular dichroism evidence for the presence of burst phase intermediates on the conformational folding pathway of ribonuclease A. Biochemistry 1996, 35, 10125-33.