Slow cooperative folding of a small globular protein HPr

Biochemistry

Volumn 37, Issue 2, 1998, Pages 622-637

  Van Nuland, Nico A J ^a,b   Meijberg, Wim ^b   Warner, Jessica ^b   Forge, Vincent ^a,c   Scheek, Ruud M ^b   Robillard, George T ^b   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c CEA SACLAY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; GLOBULAR PROTEIN; GUANIDINE; HISTIDINE; PHOSPHOPROTEIN;

ARTICLE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; GUANIDINE; KINETICS; MODELS, CHEMICAL; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PROTEIN DENATURATION; PROTEIN FOLDING; SPECIES SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 0032512440     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9717946     Document Type: Article

References (65)

1. Dobson, C. M., and Ptytsin, O. B. (1997) Curr. Opin. Struct. Biol. 7, 1-2.
2. Plaxco, K. W., and Dobson, C. M. (1996) Curr. Opin. Struct. Biol. 6, 630-636.
3. Balbach, J., Forge, V., Van Nuland, N. A. J., Winder, S. L., Hore, P. J., and Dobson, C. M. (1995) Nat. Struct. Biol. 2, 865-870.
4. Hoetzli, S. D., and Frieden, C. (1996) Biochemistry 35, 16843-16851.
5. Balbach, J., Forge, V., Lau, W. S., Van Nuland, N. A. J., Brew, K., and Dobson, C. M. (1996) Science 274, 1161-1163.
6. Postma, P. W., Lengeler, J. W., and Jacobson, G. R. (1993) Microbiol. Rev. 57, 543-594.
7. Hammen, P. K., Waygood, E. B., and Klevit, R. E. (1991) Biochemistry 30, 11842-11850.
8. Van Nuland, N. A. J., Grötzinger, J., Dijkstra, K., Scheek, R. M., and Robillard, G. T. (1992) Eur. J. Biochem. 210, 881-891.
9. Van Nuland, N. A. J., Hangyi I. W., Van Schaik R. C., Berendsen H. J. C., Van Gunsteren, W. F., Scheek, R. M., and Robillard, G. T. (1994) J. Mol. Biol. 237, 544-559.
10. Wittekind, M., Rajagopal, P., Baranchini, B. R., Reizer, J., Saier, M. H., Jr., and Klevit, R. E. (1992) Protein Sci. 1, 1363-1376.
11. Kalbitzer, H. R. and Hengstenberg, W. (1993) Eur. J. Biochem. 216, 205-214.
12. Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Reizer, J., and Kapafia, G. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2499-2503.
13. Jia, Z., Vandonselaar, M., Quail, J. W., and Delbaere, L. T. J. (1993) Nature 361, 94-97.
14. Jia, Z., Quail, J. W., Waygood, E. B., and Delbaere, L. T. J. (1993) J. Biol. Chem. 268, 22490-22501.
15. Pastore, A., Saudek, V., Ramponi, G., and Williams, R. J. P. (1992) J. Mol. Biol. 224, 427-440.
16. Swindells, M. B., Orengo, C. A., Jones, D. T., Pearl, L. H., and Thornton J. M. (1993) Nature 362, 299.
17. Liao, D.-I., and Herzberg, O. (1994) Structure 2, 1203-1216.
18. Miranker, A. D., and Dobson, C. M. (1996) Curr. Opin. Struct. Biol. 6, 31-42.
19. Scholtz, J. M. (1995) Protein Sci. 4, 35-43.
20. Nicholson, E. M., and Scholtz, J. M. (1996) Biochemistry 35, 11369-11378.
21. Van Nuland, N. A. J., Van Dijk, A. A., Dijkstra, K., Van Hoesel, F. H. J., Scheek, R. M., and Robillard, G. T. (1992) Eur. J. Biochem. 203, 483-491.
22. Pace, C. N (1986) Methods Enzymol. 131, 266-280.
23. Santoro, M. M., and Bolen, D. W. (1988) Biochemistry 27, 8063-8068.
24. Live, D. H., Davis, D. G., Agosta, W. C., and Cowburn, D. (1984) J. Am. Chem. Soc. 106, 1939-1941.
25. Redfield, A. G., and Kunz, S. D. (1975) J. Magn. Reson. 19, 250-254.
26. Santoro, M. M., and Bolen, D. W. (1992) Biochemistry 31, 4901-4907.
27. Pace, C. N., and Tanford, C. (1968) Biochemistry 7, 198-208.
28. Robertson, A. D., and Baldwin, R. L. (1991) Biochemistry 30, 9907-9914.
29. Agashe, V. R., and Udgaonkar, J. B. (1995) Biochemistry 34, 3286-3299.
30. Privalov, P. L. (1979) Adv. Protein Chem. 33, 167-241.
31. Dill, K. A., and Shortle, D. (1991) Annu. Rev. Biochem. 60, 795-825.
32. Gadian, D. G. (1984) Nuclear magnetic resonance and its application to living systems, Clarendon Press, Oxford.
33. Lu, H. (1996) D.Phil. Thesis, University of Oxford, Oxford, England.
34. Sharma, S., Hammen, P. K., Anderson, J. W., Leung, A., Georges, F., Hengstenberg, W., Klevit, R. E., and Waygood, E. B. (1993) J. Biol. Chem. 268, 17695-17704.
35. Mayr, L. M., Kiefhaber, T., and Schmid, F. X. (1993) in Protein Folding: In Vivo and In Vitro (Cleland, J. L., Ed.) pp 142-155, American Chemical Society, Washington, DC.
36. Chen, Y., Reizer, J., Saier, M. H., Jr., Fairbrother, W. J., and Wright, P. E. (1993) Biochemistry 32, 32-37.
37. Van Nuland, N. A. J., Kroon, G. J. A., Dijkstra, K., Wolters, G. K., Scheek, R. M., and Robillard, G. T. (1993) FEBS Lett. 315, 11-15.
38. Jackson, S. E., and Fersht, A. R. (1991) Biochemistry 30, 10436-10443.
39. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Protein Sci. 4, 2138-2148.
40. Murphy, K. P., and Freire, E. (1992) Adv. Protein Chem. 43, 313-361.
41. Makathadze, G. I., and Privalov, P. L. (1990) J. Mol. Biol. 213, 375-384.
42. Privalov, P. L., and Gill, S. J. (1988) Adv. Protein Chem. 39, 191-234.
43. Alexander, P., Fahnestock, S., Lee, T., Orban, J., and Bryan, P. (1992) Biochemistry 31, 3597-3603.
44. Brandts, J. F., Halvorson, H. R., and Brennan, M. (1975) Biochemistry 14, 4953-4963.
45. Smith, L. J., Fiebig, K. M., Schwalbe, H., and Dobson, C. M. (1996) Folding Design 5, R95-R106.
46. Fersht, A. R. (1997) Curr. Opin. Struct. Biol. 7, 3-9.
47. Shoemaker, B. A., Wang, J., and Wolynes, P. G. (1997) Proc. Nat. Acad. Sci. U.S.A. 94, 777-782.
48. Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (1995) Proteins: Struct. Funct. Genet. 3, 167-195
49. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
50. Schindler, T., Herrler, M., Marahiel, M. A., and Schmid, F. X. (1995) Nat. Struct. Biol. 2, 663-673.
51. Burton, R. E., Huang, G. S., Daugherty, M. A., Fullbright, P. W., and Oas, T. G. (1996) J. Mol. Biol. 263, 311-322.
52. Kragelund, B. B., Robinson, C. V., Knudsen, J. Dobson, C. M., and Poulsen, F. M. (1995) Biochemistry 34, 7217-7224.
53. Kragelund, B. B., Hørup, P., Jensen, M. S., Schjerling, C. K., Juul, E., Knudsen, J., and Poulsen, F. M. (1996). J. Mol. Biol. 256, 187-200.
54. Huang, G. S. and Oas, T. G. (1995). Proc. Natl. Acad. Sci. U.S.A. 92, 6878-6882.
55. Bai, Y., Karimi, A., Dyson, H. J., and Wright, P. E. (1997) Protein Sci. 6, 1449-1457.
56. Viguera, A. R., Martínez, J. C., Filimonov, V. V., Mateo, P. L., and Serrano, L. (1994) Biochemistry 33, 2142-2150.
57. Schönbrunner, N., Koller, K.-P., and Kiefhaber, T. (1997) J. Mol. Biol. 268, 526-538.
58. Jackson, S. E., and Fersht, A. R. (1991) Biochemistry 30, 10428-10435.
59. Alexander, P., Orban, J., and Bryan, P. (1992) Biochemistry 31, 7243-7248.
60. Kuszewski, J., Clore, G. M., and Gronenborn, A. M. (1994) Protein Sci. 3, 1945-1952.
61. Villegas, A., Azuaga, A., Catasús, Ll., Reverter, D., Mateo, P. L., Avilés, F. X., and Serrano, L. (1994) Biochemistry 33, 2142-2150.
62. Waldburger, C. D., Jonsson, T., and Sauer, R. T. (1996). Proc. Natl. Acad. Sci. U.S.A. 93, 2629-2634.
63. Lee, B., and Richards, F. M. (1971) J. Mol. Biol. 55, 379-400.
64. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151-176.
65. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.