Abstract
THE α-helix was proposed by Pauling et al.1 as a stable configuration of the polypeptide chain, and considerable support for this view was obtained from the X-ray diffraction patterns yielded by naturally occurring and synthetic polypeptides2,3. The diameter of the α-helix was estimated to be about 10 Å and includes the contribution of the side-chains as well as the main-chains of the protein4. Direct proof of the existence of α-helices in the globular protein myoglobin was obtained by Fourier synthesis methods5, and there is evidence suggesting that the α-group of fibrous proteins contains rope—or cable-like assemblies of distorted α-helices4,6.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Pauling, L., Corey, R. B., and Branson, H. R., Proc. U.S. Nat. Acad. Sci. 37, 205 (1951).
Perutz, M. F., Nature, 167, 1053 (1951).
Bamford, C. H., Elliott, A., and Hanby, W. E., Synthetic Polypeptides (Acad. Press, New York, 1956).
Pauling, L., and Corey, R. B., Nature, 171, 59 (1953).
Kendrew, J. C., Dickerson, R. E., Standberg, B. E., Hart, R. G., and Davies, D. R., Nature, 185, 422 (1960).
Crick, F. H. C., Acta Cryst., 6, 689 (1953).
Dobb, M. G. (in preparation).
Fraser, R. D. B., and MacRae, T. P., J. Mol. Biol., 3, 640 (1961).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
DOBB, M. α-Helix in Fibrous Proteins. Nature 207, 293 (1965). https://doi.org/10.1038/207293a0
Issue date:
DOI: https://doi.org/10.1038/207293a0
