Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures

Biochemistry

Volumn 37, Issue 8, 1998, Pages 2538-2545

  Parker, Martin J ^a   Lorch, Mark ^a   Sessions, Richard B ^a   Clarke, Anthony R ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CD2 ANTIGEN; DISULFIDE; PHOSPHOGLYCERATE KINASE; PROLINE; PROTEIN;

AMINO ACID COMPOSITION; ARTICLE; DISULFIDE BOND; ENTHALPY; ENTROPY; FLUOROMETRY; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; RAT; THERMODYNAMICS;

ANIMALS; ANTIGENS, CD2; BACILLUS STEAROTHERMOPHILUS; ENTROPY; KINETICS; PHOSPHOGLYCERATE KINASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; RATS; RECOMBINANT PROTEINS; SOLVENTS; TEMPERATURE; THERMODYNAMICS;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0032562178     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972459k     Document Type: Article

References (51)

1. Roder, H., and Colón, W. (1997) Curr. Opin. Struct. Biol. 7, 15-28.
2. Clarke, A. R., and Waltho, J. P. (1997) Curr. Opin. Biotech. 8, 400-410.
3. Kuwajima, K. (1989) Proteins: Struct., Funct., Genet. 6, 87-103.
4. Roder, H., ElÖve, G. A., and Englander, S. W. (1988) Nature 335, 700-704.
5. Udgaonkar, J. B., and Baldwin, R. L. (1988) Nature 335, 694-699.
6. Matouschek, A., Kellis, J. T., Serrano, L., Bycroft, M., and Fersht, A. R. (1990) Nature 346, 440-445.
7. Khorasanizadeh, S., Peters, I. D., and Roder. H. (1996) Nat. Struct. Biol. 3, 193-205.
8. Parker, M. J., Sessions, R. B., Badcoe, I. G., and Clarke, A. R. (1996) Folding Des. 1, 145-156.
9. Fersht, A. R., Serrano, L., and Matouschek, A. (1992) J. Mol. Biol. 224, 771-782.
10. Fersht, A. R. (1995) Curr. Opin. Struct. Biol. 5, 79-84.
11. Makhatadze, G. I., and Privalov, P. L. (1990) J. Mol. Biol. 213, 375-384.
12. Makhatadze, G. I., and Privalov, P. L. (1993) J. Mol. Biol. 232, 639-659.
13. Privalov, P. L., and Makhatadze, G. I. (1993) J. Mol. Biol. 232, 660-679.
14. Griko, Y. V., Makhatadze, G. I., Privalov, P. L., and Hartley, R. W. (1994) Protein Sci. 3, 669-676.
15. Chen, B. L., Baase, W. A., and Schellman, J. A. (1989) Biochemistry 28, 691-699.
16. Chen, X., and Matthews, C. R. (1994) Biochemistry 33, 6356-6362.
17. Oliveberg, M., and Fersht, A. R. (1996) Biochemistry 35, 2738-2749.
18. Schindler, T., and Schmid, F. X. (1996) Biochemistry 35, 16833-16842.
19. Segawa, S., and Sugihara, M. (1984) Biopolymers 23, 2473-2488.
20. Tan, Y. J., Oliveberg, M., and Fersht, A. R. (1996) J. Mol. Biol. 264, 377-389.
21. Hosszu, L. L. P., Craven, C. J., Spencer, J., Parker, M. J., Clarke, A. R., Kelly, M., and Waltho, J. P. (1997) Biochemistry 36, 333-340.
22. Driscoll, P. C., Cyster, J. G., Campbell, I. D., and Williams, A. F. (1991) Nature 353, 762-765.
23. Parker, M. J., Spencer, J., and Clarke, A. R. (1995) J. Mol. Biol. 253, 771-786.
24. Parker, M. J., and Clarke, A. R. (1997) Biochemistry 36, 5786-5794.
25. Hosszu, L. L. P., Craven, C. J., Parker, M. J., Lorch, M., Spencer, J., Clarke, A. R., and Waltho, J. P. (1997) Nature Struct. Biol. 4, 801-804.
26. Parker, M. J., Dempsey, C. E., Lorch, M., and Clarke, A. R. (1997) Biochemistry 36, 13396-13405.
27. Itzhaki, L. S., Otzen, D. E., and Fersht, A. R. (1995) J. Mol. Biol. 254, 260-288.
28. Jackson, S. E., el Masry, N., and Fersht, A. R. (1993) Biochemistry 32, 11270-11278.
29. Serrano, L., Matouschek, A., and Fersht, A. R. (1992) J. Mol. Biol. 224, 805-818.
30. Serrano, L., Kellis, J. T., Cann, P., and Matouschek, A. (1992) J. Mol. Biol. 224, 783-804.
31. Hernàndez, E. L., and Serrano, L. (1996) Folding Des. 1, 43-55.
32. Yamasaki, K., Ogasahura, K., Yutani, K., Oobatake, M., and Kanaya, S. (1995) Biochemistry 34, 16552-16562.
33. Milla, M. E., Brown, B. M., Waldburger, C. D., and Sauer, R. T. (1995) Biochemistry 34, 13914-13919.
34. Johnson, C. M., and Fersht, A. R. (1995) Biochemistry 34, 6795-6804.
35. Shortle, D., Meeker, A. K., and Freire, E. (1988) Biochemistry 27, 4761-4768.
36. Staniforth, R. A., Burston, S. G., Smith, C. J., Jackson, G. S., Badcoe, I. G., Atkinson, T., Holbrook, J. J., and Clarke, A. R. (1993) Biochemistry 32, 3842-3851.
37. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Protein Sci. 4, 2138-2148.
38. Schellman, J. A. (1955) Trav. Lab. Carlsberg, Ser. Chim. 29, 223-229.
39. Frank, H. S., and Evans, M. W. (1945) J. Chem. Phys. 13, 507-515.
40. Gill, S. J., Dec, S. F., Olofsson, G., and Wadso, I. (1985) J. Phys. Chem. 89, 3758-3765.
41. Muller, N. (1990) Acc. Chem. Res. 23, 23-28.
42. Nemethy, G., and Scheraga, H. A. (1962) J. Chem. Phys. 36, 3401-3408.
43. Spolar, R. S., Livingstone, J. R., and Record, M. T., Jr. (1992) Biochemistry 31, 3947-3955.
44. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
45. Alonso, D. O. V., and Dill, K. A. (1991) Biochemistry 30, 5974-5985.
46. Kiefhaber, T. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 9029-9033.
47. Mirny, L. A., Abkevich, V., and Shakhnovich, E. I. (1996) Folding Des. 1, 103-116.
48. Rank, J. A., and Baker, D. (1997) Protein Sci. 6, 347-354.
49. Weast, R. C. (1989) Handbook of Chemistry and Physics, 70th ed., CRC Press, Boca Raton, FL.
50. Hagen, S. J., Hofrichter, J., Szabo, A., and Eaton, W. A. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 11615-11617.
51. Matouschek, A., and Fersht, A. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 7814-7818.