Acid-induced molten globule state of a fully active mutant of human interleukin-6

Biochemistry

Volumn 35, Issue 35, 1996, Pages 11503-11511

  De Filippis, Vincenzo ^a   De Laureto, Patrizia Polverino ^a   Toniutti, Nicoletta ^a   Fontana, Angelo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; INTERLEUKIN 6; MUTANT PROTEIN; UREA;

ARTICLE; CONTROLLED STUDY; HUMAN; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

AMINO ACID SEQUENCE; ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; ENDOPEPTIDASES; FLUORESCENT DYES; HUMANS; HYDROGEN-ION CONCENTRATION; INTERLEUKIN-6; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; TEMPERATURE; UREA;

STAPHYLOCOCCUS AUREUS;

EID: 0029757518     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9604587     Document Type: Article

References (80)

1. Balbach, J., Forge, V., van Nuland, N. A., Winder, S. L., Hore, P. J., & Dobson, C. M. (1995) Nat. Struct. Biol. 2, 865-870.
2. Barrick, D., & Baldwin, R. L. (1993) Biochemistry 32, 3790-3796.
3. Bazan, J. F. (1991) Neuron 7, 197-208.
4. Breton, J., La Fiura, A., Bertolero, F., Orsini, G., Valsassina, B., Ziliotto, R., De Filippis, V., Polverino de Laureto, P., & Fontana, A. (1995) Eur. J. Biochem. 227, 573-581.
5. Brunger, A. T. (1990) X-PLOR, Manual version 2.1, Yale University, New Haven, CT.
6. Bychkova, V. E., Pain, R. H., & Ptitsyn, O. B. (1988) FEBS Lett. 238, 231-234.
7. Bychkova, V. E., Berni, R., Rossi, G. L., Kutyshenko, V. P., & Ptitsyn, O. B. (1992) Biochemistry 31, 7566-7571.
8. Carra, J. H., Anderson, E. A., & Privalov, P. L. (1994) Biochemistry 33, 10842-10850.
9. Corbett, R. J. T., & Roche, R. S. (1984) Biochemistry 23, 1888-1894.
10. Creighton, T. E. (1979) J. Mol. Biol. 129, 235-264.
11. De Filippis, V., Sander. C. & Vriend, G. (1994) Protein Eng. 7, 1203-1208.
12. Dill, K. A., & Shortle, D. (1991) Annu. Rev. Biochem. 60, 795-825.
13. Dill, K. A., Bromberg, S., Yue, K., Fiebig, K. M., Yee, D. P., Thomas, P. D., & Chan, H. S. (1995) Protein Sci. 4, 561-601.
14. Dobson, C. M. (1992) Curr. Opin. Struct. Biol. 2, 6-12.
15. Dobson, C. M. (1994) Curr. Biol. 4, 636-640.
16. Drapeau, G. R. (1977) Methods Enzymol. 47, 189-191.
17. Evans, P. A., Topping, K. D., Woolfson, D. N., & Dobson, C. M. (1991) Proteins: Struct., Funct., Genet. 9, 248-266.
18. Ewbank, J. J., Creighton, T. E., Hayer-Hartl, M. K., & Hartl, F. U. (1995) Nat. Struct. Biol. 2, 10.
19. Feng, Y., Sligar, S. G., & Wand, A. J. (1994) Nat. Struct. Biol. 1, 30-35.
20. Fink, A. L. (1995) Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
21. Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T., & Palleros, D. R. (1994) Biochemistry 33, 12504-12511.
22. Finkelstein, A. V., & Shakhnovich, E. I. (1989) Biopolymers 28, 1681-1694.
23. Fontana, A., Polverino de Laureto, P., & De Filippis, V. (1993) in Stability and Stabilization of Enzymes (van den Tweel, W. J. J., Harder, A., & Buitelaar, R. M., Eds.) pp 101-110, Elsevier, Amsterdam.
24. Freire, E. (1995) Annu. Rev. Biophys. Biomol. Struct. 24, 141-165.
25. Fruton, J. S. (1987) in Hydrolytic Enzymes (Neuberger, A., & Brocklehurst, K., Eds.) pp 132-145. Elsevier, Amsterdam.
26. Gill, S. C., & von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326.
27. Goto, Y., & Fink, A. L. (1990) J. Mol Biol. 214, 803-805.
28. Goto, Y., Takahashi, N., & Fink, A. L. (1990) Biochemistry 29, 3486-3488.
29. Griko, Y. V., Freire, E., & Privalov, P. L. (1994) Biochemistry 33, 1889-1899.
30. Hammacher, A., Ward, L. D., Weinstock, J., Trentlein, H., Yasukawa, K., & Simpson, R. J. (1994) Protein Sci. 3, 2280-2293.
31. Haynie, D. T., & Freire, E. (1993) Proteins: Struct., Funct., Genet. 16, 115-140.
32. Ichikawa, T., & Terada, H. (1979) Biochim. Biophys. Acta 580, 120-128.
33. Jennings, P. A., & Wright, P. E. (1993) Science 262, 892-896.
34. Khurana, R., & Udgaokar, J. B. (1994) Biochemistry 33, 106-115.
35. Kiefhaber, T., & Baldwin, R. L. (1995) J. Mol. Biol. 252, 122-132.
36. Kim, P. S., & Baldwin, R. L. (1990) Annu. Rev. Biochem. 59, 631-660.
37. Kishimoto, T., & Hirano, T. (1988) Annu. Rev. Immunol. 6, 485-512.
38. Kraulis, P. (1991) J. App. Crystallogr. 24, 946-950.
39. Kuwajima, K. (1989) Proteins: Struct., Funct., Genet. 6, 87-103.
40. Lakowicz, J. R. (1986) in Principles of Fluorescence Spectroscopy (Lakowicz, J. R., Ed.) pp 341-381, Plenum Press. New York.
41. Lovejoy, B., Cascio, D., & Eisenberg, D. (1993) J. Mol. Biol. 234, 640-653.
42. Lumry, R., Biltonen, R. L., & Brandts, J. F. (1966) Biopolymers 4, 917-945.
43. Miranker, A. D., & Dobson, C. M. (1996) Curr. Opin. Struct. Biol. 6, 31-42.
44. Morozova, L. A., Haynie, D. T., Arico-Muendel, C., van Dael, H., & Dobson, C. M. (1995) Nat. Struct. Biol. 2, 871-875.
45. Nishii, I., Kataoka, M., & Goto, Y. (1995) J. Mol. Biol. 250, 223-238.
46. Nishimura, C., Hanzawa, H., Itoh, S., Yasukawa, K., Shimada, I., Kishimoto, T., & Arata, Y. (1990) Biochim. Biophys. Acta 1041, 243-249.
47. Nishimura, C., Watanabe, A., Gouda, H., Shimada, I., & Arata, Y. (1996) Biochemistry. 35, 273-281.
48. Okazaki, A., Ikura, T., & Kuwajima, K. (1995) Nat. Struct. Biol. 2, 10-11.
49. Pace, C. N. (1986) Methods Enymol. 131, 266-279.
50. Paonessa, G., Graziani, R., De Serio, A., Savino, R., Ciapponi, L., Salvati, A. L., Toniatti, C., & Ciliberto, G. (1995) EMBO J. 14, 1942-1951.
51. Peng, Z.-Y., & Kim, P. S. (1994) Biochemistry 33, 2131-2141.
52. Pfeil, W. (1993) Protein Sci. 2, 1497-1501.
53. Ptitsyn, O. B. (1992) in Protein Folding (Creighton, T. E., Ed.) pp 243-300, W. H. Freeman & Co., New York.
54. Ptitsyn, O. B. (1995a) Adv. Protein Chem. 47, 83-229.
55. Ptitsyn, O. B. (1995b) FEBS Lett. 20, 376-379.
56. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, R., & Razgulajev, O. I. (1990) FEBS Lett. 262, 20-24.
57. Ragone, R., Colonna, G., Balestrieri, C., Servillo, L., & Irace, G. (1984) Biochemistry 23, 1871-1875.
58. Redfield, C., Smith, R. A. G., & Dobson, C. M. (1994) Nat. Struct. Biol. 1, 23-29.
59. Robertson, A. D., & Baldwin, R. L. (1991) Biochemistry 30, 9907-9914.
60. Robson, B., & Pain, R. H. (1976) Biochem. J. 155, 331-334.
61. Rock, L. R., Li, X., Chong, P., Ida, N., & Klein, M. (1994) Biochemistry 33, 5146-5154.
62. Rossi Fanelli, A., Antonini, E., & Caputo, A. (1958) Biochim. Biophys. Acta 30, 608-615.
63. Savino, R., Lahm, A., Salvati, A. L., Ciapponi, L., Sporeno, E., Altamura, S., Paonessa, G., Toniatti, C., & Ciliberto, G. (1994) EMBO J. 13, 1357-1367.
64. Scholtz, J. M., Qian, H., York, E. J., Stewart, J. M., & Baldwin, R. L. (1991) Biopolymers 31, 1463-1470.
65. Scholtz, J. M., Barrick, D., York, E. J., Stewart, J. M., & Baldwin, R. L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 185-189.
66. Shakhnovich, E. I., & Finkeistein, A. V. (1989) Biopolimers 28, 1667-1680.
67. Silver, I. A., Murrils, R. J., & Etherington, D. J. (1988) Exp. Cell. Res. 175, 266-267.
68. Strickland, E. H. (1974) CRC Crit. Rev. Biochem. 3, 113-175.
69. Tanford, C. (1968) Adv. Protein Chem. 23, 121-282.
70. Thomas, P. J., Qu, B.-H., & Pedersen, P. L. (1995) Trends Biol. Sci. 20, 456-459.
71. Toumadje, A., Alcorn, S. W., & Johnson, W. C., Jr. (1992) Anal. Biochem. 200, 321-331.
72. van Snick, J. (1990) Annu. Rev. Immunol. 8, 253-279.
73. Vriend, G. (1990) J. Mol. Graph. 8, 52-56.
74. Ward, L. D., Zhang, J.-G., Checkley, G., Preston, B., & Simpson, R. J. (1993) Protein Sci. 2, 1291-1300.
75. Ward, L. D., Matthews, J. M., Zhang, J.-G., & Simpson, R. J. (1995) Biochemistry 34, 11652-11659.
76. Weber, G., & Young, L. B. (1964) J. Biol. Chem. 239, 1415-1423.
77. Wong, K.-P., & Tanford, C. (1973) J. Biol. Chem. 248, 8518-8523.
78. Xie, D., Fox, R., & Freire, E. (1994) Protein Sci. 3, 2175-2184.
79. Yutani, K., Ogasahara, K., & Kuwajima, K. (1992) J. Mol. Biol. 228, 347-350.
80. Zink, T., Ross, A., Luers, K., Cieslar, C., Rudolph, R., & Holak, T. A. (1994) Biochemistry 33, 8453-8463.