A lysine 73 → histidine variant of yeast iso-1-cytochrome c: Evidence for a native-like intermediate in the unfolding pathway and implications for m value effects

Biochemistry

Volumn 36, Issue 1, 1997, Pages 119-126

  Godbole, Shubhada ^a   Dong, Aichun ^b   Garbin, Kristen ^a   Bowler, Bruce E ^a  

^a UNIVERSITY OF DENVER   (United States)

^b UNIVERSITY OF NORTHERN COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; CYC1 PROTEIN, S CEREVISIAE; FUNGAL PROTEIN; GUANIDINE; GUANIDINE DERIVATIVE; SACCHAROMYCES CEREVISIAE PROTEIN; TRYPTOPHAN; UREA;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS; CHEMICAL STRUCTURE; CHEMISTRY; FLUORESCENCE; GENETICS; INFRARED SPECTROSCOPY; METABOLISM; PH; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY;

CIRCULAR DICHROISM; CYTOCHROME C GROUP; CYTOCHROMES C; FLUORESCENCE; FUNGAL PROTEINS; GUANIDINE; GUANIDINES; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROPHOTOMETRY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TRYPTOPHAN; UREA;

EID: 0030614407     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961915m     Document Type: Article

References (52)

1. Anfinsen, C. B. (1973) Science 181, 223-230.
2. Babul, J., & Stellwagen, E. (1971) Biopolymers 10, 2359-2361.
3. Babul, J., & Stellwagen, E. (1972) Biochemistry 11, 1195-1200.
4. Bai, Y., & Englander, S. W. (1996) Proteins: Struct., Funct., Genet. 24, 145-151.
5. Bai, Y., Sosnick, T. R., Mayne, L., & Englander, S. W. (1995) Science 269, 192-197.
6. Barrick, D., Hughson, F. M., & Baldwin, R. L. (1994) J. Mol. Biol. 237, 588-601.
7. Berghuis, A. M., & Brayer, G. D. (1992) J. Mol. Biol. 223, 959-976.
8. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Jr., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
9. Betz, S. F., & Pielak, G. J. (1992) Biochemistry 31, 12337-12344.
10. Bowler, B. E., May, K., Zaragoza, T., York, P., Dong, A., & Caughey, W. S. (1993) Biochemistry 32, 183-190.
11. Bowler, B. E., Dong, A., & Caughey, W. S. (1994) Biochemistry 33, 2402-2408.
12. Carra, J. H., & Privalov, P. (1995) Biochemistry 34, 2034-2041.
13. Carra, J. H., Anderson, E. A., & Privalov, P. (1994) Biochemistry 33, 10842-10850.
14. Chignell, D., Azhir, A., & Gratzer, W. (1972) Eur. J. Biochem. 26, 37-42.
15. Christianson, T. W., Sikorski, R. S., Dante, M., Shero, J. H., & Hieter, P. (1992) Gene 110, 119-122.
16. Dill, K. A., & Shortle, D. (1991) Annu. Rev. Biochem. 60, 795-825.
17. Dong, A., Huang, P., & Caughey, W. S. (1992) Biochemistry 31, 182-189.
18. Elove, G. A., Bhuyan, A. K., & Roder, H. (1994) Biochemistry 33, 6925-6935.
19. Elwell, M. L., & Schellman, J. A. (1979) Biochim. Biophys. Acta 580, 327-338.
20. Fauchere, J. L., & Pliska, V. (1983) Eur. J. Med. Chem. 18, 369-375.
21. Freedman, R. B. (1992) in Protein Folding (Creighton, T. E., Ed.) pp 455-540, W. H. Freeman & Co., New York.
22. Griko, Y. V., Freire, E., & Privalov, P. L. (1994) Biochemistry 33, 1889-1899.
23. Hawkins, B. K., Hilgen-Willis, S., Pielak, G. J., & Dawson, J. H. (1994) J. Am. Chem. Soc. 116, 3111-3112.
24. Herrmann, L., Bowler, B. E., Dong, A., & Caughey, W. S. (1995) Biochemistry 34, 3040-3047.
25. Herrmann, L., Flatt, P., & Bowler, B. E. (1996) Inorg. Chim. Acta 242, 97-103.
26. Hughson, F. M., & Baldwin, R. L. (1989) Biochemistry 28, 4415-4422.
27. Hughson, F. M., Wright, P. E., & Baldwin, R. L. (1990) Science 249, 1544-1548.
28. Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165-184.
29. Koshy, T. I., Luntz, T. L., Schejter, A., & Margoliash, E. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 8697-8701.
30. Louie, G. V., & Brayer, G. D. (1990) J. Mol. Biol. 214, 537-555.
31. Lowenthal, R., Sancho, J., & Fersht, A. R. (1992) J. Mol. Biol. 224, 759-770.
32. Matouschek, A., & Fersht, A. R. (1994) Methods Enzymol. 202, 83-112.
33. Matthews, B. W. (1993) Annu. Rev. Biochem. 62, 139-160.
34. Mayo, S. (1938) Ph.D. Thesis, California Institute of Technology.
35. Moore, G. R., & Pettigrew, G. W. (1990) in Cytochrome c: Evolutionary, Structural and Physicochemical Aspects (Moore, G. R., & Pettigrew, G. W., Eds.) Springer-Verlag, Berlin.
36. Muthukrishnan, K., & Nall, B. T. (1991) Biochemistry 30, 4706-4710.
37. Myer, Y. P. (1968) Biochemistry 7, 765-776.
38. Neri, D., Billeter, M., Wider, G., & Wuthrich, K. (1992) Science 257, 1559-1563.
39. Oliveberg, M., Vuilleumier, S., & Fersht, A. R. (1994) Biochemistry 33, 8826-8832.
40. Pace, C. N. (1975) CRC Crit Rev. Biochem. 3, 1-43.
41. Pakula, A. A., & Sauer, R. T. (1990) Nature 344, 363-364.
42. Qin, W. T., Sanishvili, R., Plotkin, B., Schejter, A., & Margoliash, E. (1995) Biochim. Biophys. Acta 1252, 87-94.
43. Saab-Rincon, G., Froebe, C. L., & Matthews, C. R. (1993) Biochemistry 32, 13981-13990.
44. Saab-Rincon, G., Gualfetti, P. J., & Matthews, C. R. (1996) Biochemistry 35, 1988-1994.
45. Schejter, A., & George, P. (1964) Biochemistry 3, 1045-1049.
46. Schellman, J. A. (1978) Biopolymers 17, 1305-1322.
47. Shortle, D. (1995) Adv. Protein Chem. 46, 217-247.
48. Shortle, D., & Meeker, A. K. (1986) Proteins: Struct., Funct., Genet. 1, 81-89.
49. Sosnick, T. R., Mayne, L., Hiller, R., & Englander, S. W. (1994) Nature, Struct. Biol. 1, 149-156.
50. Tsong, T. Y. (1973) Biochemistry 12, 2209-2214.
51. Tsong, T. Y. (1974) J. Biol Chem. 249, 1988-1990.
52. Tsong, T. Y. (1975) Biochemistry 14, 1542-1547.