Temperature-jump induced fast refolding of cold-unfolded protein

Biochemical and Biophysical Research Communications

Volumn 227, Issue 3, 1996, Pages 903-908

  Nölting, Bengt ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTOGLOBULIN;

ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY;

BOVINAE;

EID: 0030599429     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.1603     Document Type: Article

References (25)

1. 1. Nölting, B., Golbik, R., and Fersht, A. R. (1995) Proc. Natl. Acad. Sci. USA 92, 10668-10672.
2. 2. Ballew, R. M., Sabelko, J., and Gruebele, M. (1996) Proc. Natl. Acad. Sci. USA 93, 5759-5764.
3. 3. Matouschek, A., Kellis, J. T., Jr., Serrano, L., Bycroft, M., and Fersht, A. R. (1990) Nature (London) 346, 440-445.
4. 4. Pfeil, W., Nölting, B., and Jung, C. (1993a) Biochemistry 32, 8856-8862.
5. 5. Pfeil, W., Nölting, B., and Jung, C. (1993b) Stability and Stabilization of Enzymes (van den Tweel, W. J. J., Harder, A., and Buitelaar, R. M., Eds.), pp. 407-414, Elsevier.
6. 6. Fersht, A. R. (1993) FEBS Lett. 325, 5-16.
7. 7. Fersht, A. R. (1995a) Curr. Opin. Struct. Biol. 5, 79-84.
8. 8. Nölting, B., and Fersht, A. R. (1995) Biophys. J. 68, A183.
9. 9. Kiefhaber, T., Labhardt, A. M., and Baldwin, R. L. (1995) Nature (London) 375, 513-515.
10. 10. Jamieson, A. C., Vandeyar, M. A., Kang, Y. C., Kinsella, J. E., and Batt, C. A. (1987) Gene 61, 85-90.
11. 11. Cho, Y., Gu, W., Watkins, S., Lee, S., Kim, T., Brady, J. W., and Batt, C. A. (1994) Protein Engineering 7, 263-270.
12. 12. Griko, Y. V., and Privalov, P. L. (1992) Biochemistry 31, 8810-8815.
13. 13. Eigen, M., and de Maeyer, L. (1963) in Techniques of Organic Chemistry (Friess, S. L., Lewis, E. S., and Weissberger, A., Eds.), Vol. 8, part 2, pp. 895-1054, Wiley Interscience, New York.
14. 14. French, T. C., and Hammes, G. G. (1969) Methods Enzymol. 16, 3-30.
15. 15. Sligar, S. G. (1976) Biochemistry 15, 5399-5406.
16. 16. Nölting, B. (1995) J. Theor. Biol 175, 191-196.
17. 17. Eftink, M. R. (1994) Biophys. J. 66, 482-501.
18. 18. Pace, N. C., and Tanford, C. (1968) Biochemistry 7, 198-207.
19. 19. Fersht, A. R. (1985) Enzyme Structure and Mechanism, 2nd ed., Freeman, New York.
20. 20. Nölting, B., Jiang, M., and Sligar, S. G. (1993) J. Am. Chem. Soc. 115, 9879-9882.
21. 21. Nölting, B., and Sligar, S. G. (1993) Biochemistry 32, 12319-12323.
22. 22. Wei, Y., and Sridhar, S. (1991) IEEE Trans. Microwave Theory Tech. 39, 526-531.
23. 23. Matouschek, A., Kellis, J. T., Jr., Serrano, L., and Fersht, A. R. (1989) Nature (London) 340, 122-126.
24. 24. Fersht, A. R., Matouschek, A., and Serrano, L. (1992) J. Mol. Biol. 224, 771-782.
25. 25. Fersht, A. R. (1995b) Phil. Trans. R. Soc. Lond. B 348, 11-15.