Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 7, 1996, Pages 2629-2634

  Waldburger, Carey D ^a   Jonsson, Thorlakur ^a   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Arc repressor; diffusion limit; folding intermediate; refolding kinetics; transition state

Indexed keywords

ARTICLE; GENE EXPRESSION; HYDROGEN BOND; HYDROPHOBICITY; IONIC STRENGTH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; VISCOSITY;

AMINO ACID SEQUENCE; ARGININE; CALORIMETRY; DNA-BINDING PROTEINS; GLUTAMIC ACID; HYDROGEN BONDING; KINETICS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OSMOLAR CONCENTRATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; SPECTROMETRY, FLUORESCENCE; UREA; VIRAL PROTEINS; VISCOSITY;

EID: 0029966342     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.7.2629     Document Type: Article

References (28)

1. Huans, G. S. & Oas, T. G. (1995) Proc. Nutl. Acad. Sci. USA 92, 6878-6882.
2. Schindler, T., Herrler, M., Marahiel, M. A. & Schmid, F. X. (1995) Nat. Struct. Biol. 2, 663-673.
3. Bryan, P., Alexander, P., Strausberg, S., Schwarz, F., Lan, W., Gilliand, G. & Gallagher, D. T. (1992) Biochemistry 31, 4937-4945.
4. Creighton, T. E. (1986) Methods Enzymol. 131, 83-106.
5. Schmid, F. X. (1993) Annu. Rev. Biophys. Biomol. Struct. 22, 123-143.
6. Vershon, A. K., Youderian, P., Susskind, M. M. & Sauer, R. T. (1985) J. Biol. Chem. 260, 12124-12129.
7. Breg, J. N., van Opheusden, J. H. J., Burgering, M. J., Boelens, R. & Kaptein, R. (1990) Nature (London) 346, 586-589.
8. Bowie, J. U. & Sauer, R. T. (1989) Biochemistry 28, 7139-7143.
9. Milla, M. E. & Sauer. R. T. (1994) Biochemistry 33, 1125-1133.
10. Bonvin, A. M., Vis, H., Breg, J. N., Burgering, M. J., Boelens, R. & Kaptein, R. (1994). J. Mol. Biol. 236, 328-341.
11. Raumann, B. E., Rould, M. A., Pabo, C. O. & Sauer, R. T. (1994) Nature (London) 367, 754-757.
12. Waldhurger, C. D., Schildbach, J. F. & Sauer, R. T. (1995) Nat. Struct. Biol. 2, 122-128.
13. Milla, M. E., Brown, B. M. & Sauer, R. T. (1993) Protein Sci. 2, 2198-2205.
14. Brown, B. M., Milla, M. E., Smith. T. L. & Sauer, R. T. (1994) Nat. Struct. Biol. 1, 164-168.
15. Johnson, M. & Frasier, S. (1985) Methods Enzymol. 117, 301-342. ;
16. Brenstein, R. J. (1989) NONUN (Robclko Software, Carbondale, IL), version 0.9 8b5.
17. Chen, B., Baase, W. & Schellman, J. A. (1989) Biochemistry 28, 691-699.
18. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
19. Matouschek, A. & Fersht, A. R. (1993 ) Proc. Nutl. Acad. Sci. USA 90, 7814-7818.
20. Berg, O. G. & von Hippel, P. H. (1985) Annu. Rev. Biophys. Biophys. Chem. 14, 131-160.
21. Milla, M. E., Brown, B. M., Waldburger, C. D. & Sauer, R. T. (1995) Biochemistry 34, 13914-13919.
22. Burgering, M. J., Hald, M., Boelens, R., Breg, J. N. & Kaptein, ' R. (1995) Biopolymers 35, 217-226.
23. Peng, X., Jonas, J. & Silva, J. L. (1993) Proc. Nutl. Acad. Sci. USA 90, 1776-1780.
24. Matthews, C. R. (1993) Annu. Rev. Biochem. 62, 653-683.
25. Rashin, A. A. & Honig, B. (1984) J. Mol. Biol. 173, 515-521.
26. Rozwarski, D. A., Gronenborn, A. M., Clore, G. M., Bazan, J. F., Bohm, A., Wlodawer, A., Hatada, M. & Karplus, P.A. (1994) Structure 2, 159-173.
27. Sosnick, T. R., Mayne, L., Hiller, R. & Englander, S. W. (1994) Nat. Struct. Biol. 1, 149-155.
28. Jonsson, T., Waldburger, C. & Sauer, R. T. (1996) Biochemistry, in press.