Abstract
ALL recent work1–6 has confirmed that the structure of the synthetic polypeptide poly-γ-methyl-L-glutamate is based on the α-helix of Pauling and Corey7. This structure gives a strong 1.5-A. reflexion on the meridian, and both MacArthur8 and Perutz1 have shown that this reflexion also occurs in α-keratin. This suggests forcibly that the α-helix forms an important part of α-keratin.
Similar content being viewed by others
References
Perutz, M. F., Nature, 167, 1053 (1951).
Cochran, W., and Crick, F. H. C., Nature, 169, 234 (1952).
Bamford, C. H., Brown, L., Elliott, A., Hanby, W. E., and Trotter, I. F., Nature, 169, 357 (1952).
Yakel, H. L., Pauling, L., and Corey, R. B., Nature, 169, 920 (1952).
Fraser, R. D. B., and Price, W. C., Nature, 170, 490 (1952).
Cochran, W., Crick, F. H. C., and Vand, V., Acta Cryst., 5, 581 (1952).
Pauling, L., and Corey, R. B., Proc. U.S. Nat. Acad. Sci., 37, 241 (1951).
MacArthur, I., Nature, 152, 38 (1943).
Bear, R. S., J. Amer. Chem. Soc., 65, 1784 (1943).
Davies, M., Ann. Rep. Chem. Soc., 43, 1 (1946).
Crick, F. H. C., Acta Cryst., 5, 381 (1952).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
CRICK, F. Is α-Keratin a Coiled Coil?. Nature 170, 882–883 (1952). https://doi.org/10.1038/170882b0
Issue Date:
DOI: https://doi.org/10.1038/170882b0
- Springer Nature Limited
We’re sorry, something doesn't seem to be working properly.
Please try refreshing the page. If that doesn't work, please contact support so we can address the problem.