Abstract
IT is now well established that in the solid state many preparations of synthetic polypeptides form stable helical structures which correspond closely to the α-helix described by Pauling, Corey and Branson1. With other preparations, however, the α-helical configuration appears to be less stable, apparently due either to a low degree of polymerization2 or to the nature of the side-chain3. In the case of poly-β-benzyl-L-aspartate4,5 steric interference between the side-chain and main-chain renders the α-helical configuration comparatively unstable, and on heating films in vacua the molecules adopt a new helical form resembling the 413 configuration described by Bragg, Kendrew and Perutz6. The new configuration, which has been termed the ω-helix, has a pitch of 5.30 Å. with four residues per turn and is believed to be of opposite screw sense to the α-helix. We are at present investigating synthetic polypeptides with side-chains which are derivatives of cysteine and wish to report the discovery of a second example of a four residue per turn helix which closely resembles, but is not identical with, that found in poly-β-benzyl-L-aspartate.
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Pauling, L., Corey, R. B., and Branson, H. R., Proc. U.S. Nat. Acad. Sci., 37, 205 (1951).
Bradbury, E. M., Brown, L., Downie, A. R., Elliott, A., Eraser, R. D. B., Hanby, W. E., and McDonald, T. R., J. Mol. Biol., 2, 276 (1960).
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Bradbury, E. M., Brown, L., Downie, A. R., Elliott, A., Hanby, W. E., and McDonald, T. R. R., Nature, 183, 1736 (1959).
Bradbury, E. M., Brown, L., Downie, A. R., Elliott, A., Fraser, R. D. B., and Hanby, W. E., J. Mol. Biol. (in the press).
Bragg, W. L., Kendrew, J. C., and Perutz, M. F., Proc. Roy. Soc. A, 203, 321 (1950).
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FRASER, R., MACRAE, T. & STAPLETON, I. ω-Helix in Synthetic Polypeptides. Nature 193, 573 (1962). https://doi.org/10.1038/193573a0
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DOI: https://doi.org/10.1038/193573a0
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