Letter | Published:

ω-Helix in Synthetic Polypeptides

Nature volume 193, page 573 (10 February 1962) | Download Citation

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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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References

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Affiliations

  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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https://doi.org/10.1038/193573a0

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