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ω-Helix in Synthetic Polypeptides

Naturevolume 193page573 (1962) | Download Citation



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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  1. 1

    Pauling, L., Corey, R. B., and Branson, H. R., Proc. U.S. Nat. Acad. Sci., 37, 205 (1951).

  2. 2

    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).

  3. 3

    Blout, E. R., de Lozé, C., Bloom, S. M., and Fasman, G. D., J. Amer. Chem. Soc., 82, 3787 (1960).

  4. 4

    Bradbury, E. M., Brown, L., Downie, A. R., Elliott, A., Hanby, W. E., and McDonald, T. R. R., Nature, 183, 1736 (1959).

  5. 5

    Bradbury, E. M., Brown, L., Downie, A. R., Elliott, A., Fraser, R. D. B., and Hanby, W. E., J. Mol. Biol. (in the press).

  6. 6

    Bragg, W. L., Kendrew, J. C., and Perutz, M. F., Proc. Roy. Soc. A, 203, 321 (1950).

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  1. Division of Protein Chemistry, Commonwealth Scientific and Industrial Research Organization, Wool Research Laboratories, Parkville, N.2, Victoria, Australia

    • R. D. B. FRASER
    • , T. P. MACRAE
    •  & I. W. STAPLETON


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