Letter | Published:

The helical s constant for alanine in water derived from template-nucleated helices

Naturevolume 352pages451454 (1991) | Download Citation

Subjects

Abstract

FORMATION of α helices from disordered polypeptides depends on the degree to which amino acids favour the helical state. The folding of helical oligopeptides can be modelled by two parameters: σ which reflects helix initiation and s which reflects propagation of a pre-existing helix and measures helical bias1,2. Scheraga has reported s values for oligopeptides of about 1.1, implying a weak helical bias for amino-acid residues3. By contrast, certain helical peptides studied by Baldwin seem to require much larger s values for alanine4. Resolution of this inconsistency requires experiments that disentangle the ease of propagation from that of initiation. In this study varying lengths of polyalanine are linked to a 'template' that initiates helical structure and permits study solely of propagation. We report here that the s value for alanine in water is close to 1, supporting the earlier results of Scheraga but not the more recent results of Baldwin.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Poland, D. & Scheraga, H. A. Theory of Helix-Coil Transitions in Biopolymers (Academic, New York, 1970).

  2. 2

    Zimm, B. H. & Bragg, J. J. chem. Phys. 31, 526–535 (1959).

  3. 3

    Scheraga, H. A. Pure appl. Chem. 50, 315–324 (1978).

  4. 4

    Marqusee, S. & Baldwin, R. L. Proc. natn. Acad. Sci. U.S.A. 86, 5286–5290 (1989).

  5. 5

    Kemp, D. S. & Curran, T. P. Tetrahedron Lett. 29, 4931–4939 (1988).

  6. 6

    Kemp, D. S. & Boyd, J. G. Pept. Proc. Am. Pept. Symp. 11, 677–679 (1990).

  7. 7

    Kemp, D. S., Curran, T. P., Boyd, J. G. & Muendel, C. C. J. org. Chem. (in the press).

  8. 8

    Karle, I. L., Flippen-Anderson, J., Sukumar, M. & Balaram, P. Proc. natn. Acad. Sci. U.S.A. 84, 5087–5091 (1987).

  9. 9

    Bundi, A. & Wuethrich, K. Biopolymers 18, 285–297 (1979).

  10. 10

    Wagner, G., Pardi, A. & Wuethrich, K. J. Am. chem. Soc. 105, 5948–5950 (1983).

  11. 11

    Pardi, A., Billeter, M. & Wuethrich, K. J. molec. Biol. 180, 741–751 (1984).

  12. 12

    Esposito, G., Carver, J. A., Boyd, J. & Campbell, I. D. Biochemistry 26, 1043–1050 (1987).

  13. 13

    Wuethrich, K., Billeter, M. & Braun, W. J. molec. Biol. 180, 715–740 (1984).

  14. 14

    Dyson, H. J., Ranee, M., Houghten, R. A., Lerner, R. A. & Wright, P. E. J. molec. Biol. 201, 161–200 (1988).

  15. 15

    Bax, A. & Davis, D. J. magn. Reson. 63, 207–213 (1985).

  16. 16

    Bothner-By, A., Stephens, R. L. & Lee, J. J. Am. chem. Soc. 106, 811–813 (1984).

  17. 17

    Kessler, H., Griesinger, C., Kerssebaum, R., Wagner, K. & Ernst, R. J. Am. chem. Soc. 109, 607–609 (1987).

  18. 18

    States, D., Habekorn, R. & Ruben, D. J. magn. Reson. 48, 286–292 (1982).

  19. 19

    Manning, M. C., Illangasekare, M. & Woody, R. W. Biophys. Chem. 31, 77–86 (1988).

  20. 20

    Bierzynsky, A., Kim, P. S. & Baldwin, R. L. Proc. natn. Acad. Sci. U.S.A. 79, 2470–2474 (1982).

  21. 21

    Dyson, H. J., Ranee, M., Houghten, R. A., Wright, P. E. & Lerner, R. A. J. molec. Biol. 201, 201–217 (1988).

Download references

Author information

Affiliations

  1. Department of Chemistry, Room 18-584, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    • D. S. Kemp
    • , James G. Boyd
    •  & Christopher C. Muendel

Authors

  1. Search for D. S. Kemp in:

  2. Search for James G. Boyd in:

  3. Search for Christopher C. Muendel in:

About this article

Publication history

Received

Accepted

Issue Date

DOI

https://doi.org/10.1038/352451a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.