Direct conversion of an oligopeptide from a β-sheet to an α-helix: A model for amyloid formation

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

Volumn 94, Issue 1, 1997, Pages 23-28

  Zhang, Shuguang ^a   Rich, Alexander ^a  

^a Massachusetts Institute of Technology   (United States)

Author keywords

biomaterials; ionic residues; repeating sequences; scrapie related diseases; temperature induced transition

Indexed keywords

AMYLOID; OLIGOPEPTIDE;

ALPHA HELIX; AQUEOUS SOLUTION; BETA CHAIN; CIRCULAR DICHROISM; CONFERENCE PAPER; COOLING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SYNTHESIS;

EID: 0031034117     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.1.23     Document Type: Article

References (38)

1. Pauling, L. C. (1961) The Nature of Chemical Bond (Cornell Univ. Press, New York), 3rd Ed.
2. Creighton, T. E. (1993) Proteins: Structures and Molecular Principles (Freeman, New York), 2nd Ed.
3. Chou, P. Y. & Fasman, G. D. (1974) Biochemistry 13, 222-245.
4. Williams, R. W., Chang, A., Juretic, D. & Loughran, S. (1987) Biochim. Biophys. Acta, 916, 200-204.
5. Minor, D. & Kim, P. S. (1994) Nature (London) 371, 264-267.
6. Xiong, H., Buckwalter, B. L., Shieh, H. M. & Hecht, M. H. (1995) Proc. Natl. Acad. Sci. USA 92, 6349-6353.
7. Kim, P. S. & Baldwin, R. L. (1990) Anna. Rev. Biochem. 59, 631-660.
8. Fersht, A. R. (1995) Proc. Natl. Acad. Sci. USA 92, 10869-10873.
9. Dill, K. A., Fiebig, K. M. & Chan H. S. (1993) Proc. Natl. Sci. USA 90, 1924-1928.
10. Dill, K. A. (1990) Biochemistry 29, 7133-7155.
11. Greenfield, N. & Fasman, G. (1969) Biochemistry 8, 4108-4116.
12. Hartman, R., Schwaner, R. C. & Hermans, J. (1974) J. Mol. Biol. 90, 415-429.
13. Brack, A. & Orgel, L. (1975) Nature (London) 256, 383-387.
14. Ihara, S., Ooi, T. & Takahashi, S. (1982) Biopolymers 21, 131-145.
15. Zhang, S., Holmes, T. Lockshin, C. & Rich, A. (1993) Proc. Natl. Acad. Sci. USA 90, 3334-3338.
16. Zhang, S., Lockshin, C., Cook, R. & Rich, A. (1994) Biopolymers 34, 663-672.
17. Zhang, S., Holmes, T. C., DiPersio, C. M., Hynes, R. O., Su, X. & Rich, A. (1995) Biomaterials 16, 1386-1393.
18. Zhang, S., Lockshin, C., Herbert, A., Winter, E. & Rich, A. (1992) EMBO J. 11, 3787-3796.
19. Chothia, C. (1973) J. Mol. Biol. 75, 295-302.
20. Manning, M. C., Illangasekare, M. & Woody, R. W. (1974) Biophys. Chem. 31, 77-86.
21. Marqusee, S. & Baldwin, R. L. (1987) Proc. Nail. Acad. Sci. USA 84, 8898-8902.
22. Marqusee, S., Robbins, V. H. & Baldwin, R. L. (1989) Proc. Natl. Acad. Sci. USA 86, 5286-5290.
23. Astbury, W. T. (1936) Nature (London) 137, 803-805.
24. Matthews, C. K. & van Holde, K. E. (1990) Biochemistry (Benjamin & Cummings, Redwood City, CA), p. 179.
25. Hol, W. G. J. (1985) Prog. Biophys. Mol. Biol. 145, 149-195.
26. Chou, P. Y. & Fasman, G. D. (1974) Biochemistry 13, 211-221.
27. Zagorski, M. G. & Barrow, C. J. (1992) Biochemistry 31, 5621-5631.
28. Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C. L. & Beyreuther, K. (1991) J. Mol. Biol. 50, 149-165.
29. Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A., Lind, M. & Selkoe, D. J. (1987) Proc. Natl. Acad. Sci. USA 84, 6953-6957.
30. Prusiner, S. B. (1991) Science 252, 1515-1517.
31. Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J.-M., Holtzman, D. M., Cohen, F., Fletterick, R. & Prusiner, S. B. (1992) Proc. Natl. Acad. Sci. USA 89, 10940-10944.
32. Huang, Z., Prusiner, S. B. & Cohen, F. E. (1996) Folding Design 1, 13-20.
33. Han, H., Weinreb, P. H. & Lansbury, P. T. (1995) Chem. Biol. 2, 163-169.
34. Safar, J., Roller, P. P., Gajdusek, D. C. & Gibbs, C. J., Jr. (1993) Protein Sci. 2, 2206-2216.
35. Carr, C. M. & Kim, P. S. (1993) Cell 73, 823-832.
36. Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. (1994) Nature (London) 371, 37-43.
37. Perutz, M. (1994) Proc. Natl. Acad. Sci. USA 91, 5355-5359.
38. Scott, K. & Perutz, M., (1995) Proc. Natl. Acad. Sci. USA 92, 6509-6513.