Fragment reconstitution of a small protein: Folding energetics of the reconstituted immunoglobulin binding domain B1 of streptococcal protein G

Biochemistry

Volumn 38, Issue 4, 1999, Pages 1203-1213

  Honda, Shinya ^a   Kobayashi, Naohiro ^b   Munekata, Eisuke ^b   Uedaira, Hatsuho ^a,c  

^a NATL INST BIOSCI HUM TECHNOL   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c RIKEN TSUKUBA INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN G; PROTEIN G;

ARTICLE; CIRCULAR DICHROISM; COVALENT BOND; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY TRANSFER; ENTHALPY; ENTROPY; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; STREPTOCOCCUS; THERMODYNAMICS;

ANTIGENS, BACTERIAL; BACTERIAL PROTEINS; BINDING SITES, ANTIBODY; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; IMMUNOGLOBULIN G; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 0033604829     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982271g     Document Type: Article

References (70)

1. Levinthal, C. (1968) J. Chim. Phys. 65, 44-45.
2. Baldwin, R. L. (1994) Nature 369, 183-184.
3. Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., and Socci, N. D. (1995) Proc. Natl. Acad. Sci. U.S.A 92, 3626-3630.
4. Wolynes, P. G., Onuchic, J. N., and Thirumalai, D. (1995) Science 267, 1619-1620.
5. Dill, K. A., and Chan, H. S. (1997) Nat. Struct. Biol. 4, 10-19.
6. Gilbert, H. F. (1994) in Mechanisms of Protein Folding (Pain, R. H., Ed.) pp 104-136, Oxford University Press, Oxford, U.K.
7. Nall, B. T. (1994) in Mechanisms of Protein Folding (Pain, R. H., Ed.) pp 80-103, Oxford University Press, Oxford, U.K.
8. Garel, J.-R. (1992) in Protein Folding (Creighton, T. E., Ed.) pp 405-454, W. H. Freeman and Company, New York.
9. Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M., Wingfield, P. T., and Clore, G. M. (1991) Science 253, 657-661.
10. Achari, A., Hale, S. P., Howard, A. J., Clore, G. M., Gronenborn, A. M., Hardman, K. D., and Whitlow, M. (1992) Biochemistry 31, 10449-10457.
11. Gallagher, T., Alexander, P., Bryan, P., and Gilliland, G. L. (1994) Biochemistry 33, 4721-4729.
12. Alexander, P., Fahnestock, S., Lee, T., Orban, J., and Bryan, P. (1992) Biochemistry 31, 3597-3603.
13. Orban, J., Alexander, P., and Bryan, P. (1994) Biochemistry 33, 5702-5710.
14. Orban, J., Alexander, P., Bryan, P., and Khare, D. (1995) Biochemistry 34, 15291-15300.
15. Alexander, P., Orban, J., and Bryan, P. (1992) Biochemistry 31, 7243-7248.
16. Kuszewski, J., Clore, G. M., and Gronenborn, A. M. (1994) Protein Sci. 3, 1945-1952.
17. Park, S. H., O'Neil, K. T., and Roder, H. (1997) Biochemistry 36, 14277-14283.
18. Kobayashi, N., Endo, S., and Munekata, E. (1993) Pept. Chem. 1992, 278-280.
19. Blanco, F. J., Rivas, G., and Serrano, L. (1994) Nat. Struct. Biol. 1, 584-590.
20. Blanco, F. J., Jimenez, M. A., Pineda, A., Rico, M., Santoro, J., and Nieto, J. L. (1994) Biochemistry 33, 6004-6014.
21. Blanco, F. J., and Serrano, L. (1995) Eur. J. Biochem. 230, 634-649.
22. Karplus, M., and Weaver, D. L. (1976) Nature 260, 404-406.
23. Kobayashi, N., Honda, S., Yoshii, H., Uedaira, H., and Munekata, E. (1995) FEBS Lett. 366, 99-103.
24. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326.
25. Honda, S., Ohashi, S., Morii, H., and Uedaira, H. (1991) Biopolymers 31, 869-876.
26. Honda, S., Morii, H., Ohashi, S., and Uedaira, H. (1991) Biochim. Biophys. Acta 1068, 81-86.
27. Honda, S., Odahara, T., Uedaira, H., and Miyake, J. (1994) Rep. Natl. Inst. Biosci. Hum.-Technol. (Jpn.) 2, 17-20.
28. Privalov, P. L. (1979) Adv. Protein Chem. 33, 167-241.
29. Kidokoro, S., and Wada, A. (1987) Biopolymers 26, 213-229.
30. Kidokoro, S., Uedaira, H., and Wada, A. (1988) Biopolymers 27, 271-297.
31. Nakagawa, T., and Oyanagi, Y. (1980) in Recent developments in statistical inference and data analysis (Matusita, K., Ed.) pp 221-225, North-Holland Pub. Co.
32. Makhatadze, G. I., and Privalov, P. L. (1995) Adv. Protein Chem. 47, 307-425.
33. Shrake, A., and Rupley, J. A. (1973) J. Mol. Biol. 79, 351-371.
34. Chothia, C. (1975) Nature 254, 304-308.
35. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. E., Jr., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., and Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
36. Chang, C. T., Wu, C.-S. C., and Yang, T. J. (1978) Anal. Biochem. 91, 13-31.
37. Muñoz, V., Thompson, P. A., Hofrichter, J., and Eaton, W. A. (1997) Nature 390, 196-199.
38. Richards, F. M., and Vithayathil, P. J. (1959) J. Biol. Chem. 234, 1459-1465.
39. Kato, I., and Anfinsen, C. B. (1969) J. Biol. Chem. 244, 1004-1007.
40. Catanzano, F., Giancola, C., Graziano, G., and Barone, G. (1996) Biochemistry 35, 13378-13385.
41. Taniuchi, H., and Anfinsen, C. B. (1971) J. Biol. Chem. 246, 2291-2301.
42. Hartley, R. W. (1977) J. Biol. Chem. 252, 3252-3254.
43. Sancho, J., and Fersht, A. R. (1992) J. Mol. Biol. 224, 741-747.
44. Saint Girons, I., Gilles, A. M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A., and Barzu, O. (1987) J. Biol. Chem. 262, 622-629.
45. Tasayco, M. L., and Carey, J. (1992) Science 255, 594-597.
46. Wu, L. C., Laub, P. B., Elove, G. A., Carey, J., and Roder, H. (1993) Biochemistry 32, 10271-10276.
47. de Prat Gay, G., and Fersht, A. R. (1994) Biochemistry 33, 7957-7963.
48. Tasayco, M. L., and Chao, K. (1995) Proteins 22, 41-44.
49. Stites, W. E. (1997) Chem. Rev. 97, 1233-1250.
50. Ohgushi, M., and Wada, A. (1983) FEBS Lett. 164, 21-24.
51. Christensen, H., and Pain, R. H. (1994) in Mechanisms of Protein Folding (Pain, R. H., Ed.) pp 55-79, Oxford University Press, Oxford, U.K.
52. Creighton, T. E. (1993) Proteins: Structures and Molecular Properties, 2nd ed., W. H. Freeman and Company, New York.
53. Kirby, A. J. (1980) Adv. Phys. Org. Chem. 17, 183-278.
54. Chau, M. H., and Nelson, J. W. (1991) FEBS Lett. 291, 296-298.
55. Goldenberg, D. P. (1985) J. Cell Biochem. 29, 321-335.
56. Creighton, T. E. (1992) in Protein Folding (Creighton, T. E., Ed.) pp 405-454, W. H. Freeman and Company, New York.
57. Kauzmann, W. (1959) Adv. Protein Chem. 14, 1-63.
58. Ooi, T., Oobatake, M., Nemethy, G., and Scheraga, H. A. (1987) Proc. Natl. Acad. Sci. U.S.A 84, 3086-3090.
59. Spolar, R. S., Ha, J. H., and Record, M. T., Jr. (1989) Proc. Natl. Acad. Sci. U.S.A 86, 8382-8385.
60. Privalov, P. L., and Makhatadze, G. I. (1990) J. Mol. Biol. 213, 385-391.
61. Murphy, K. P., and Gill, S. J. (1991) J. Mol. Biol. 222, 699-709.
62. Murphy, K. P., and Freire, E. (1992) Adv. Protein Chem. 43, 313-361.
63. Freire, E. (1993) Arch. Biochem. Biophys. 303, 181-184.
64. Oobatake, M., and Ooi, T. (1993) Prog. Biophys. Mol. Biol. 59, 237-284.
65. Kim, P. S., and Baldwin, R. L. (1982) Annu. Rev. Biochem. 51, 459-489.
66. Go, N. (1983) Annu. Rev. Biophys. Bioeng. 12, 183-210.
67. Itzhaki, L. S., Otzen, D. E., and Fersht, A. R. (1995) J. Mol. Biol. 254, 260-288.
68. Panchenko, A. R., Luthey-Schulten, Z., and Wolynes, P. G. (1996) Proc. Natl. Acad. Sci. U.S.A 93, 2008-2013.
69. de Prat-Gay, G. (1996) Protein Eng. 9, 843-847.
70. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151-176.