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Solubilities of the αII- and β-Forms of Synthetic Polypeptides: Evidence for an αII–β Transformation in the Amorphous Phase

Abstract

IN previous communications1,2 from these Laboratories, it has been shown that the molecular chains of a number of synthetic polypeptides can exist in folded and extended configurations, and the X-ray and infra-red evidence which has accumulated so far is entirely consistent with the view that the folded form has the αII-structure proposed by Ambrose and Hanby3. One purpose of this note is to bring forward evidence of a different kind which has a bearing on the structure of the molecular fold.

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References

  1. Bamford, Hanby and Happey, Nature, 164, 138, 751 (1949); Proc. Roy. Soc. (in course of publication).

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  2. Ambrose and Elliott, Nature, 165, 921 (1950); Proc. Roy. Soc. (in course of publication).

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  3. Ambrose and Hanby, Nature, 163, 483 (1949).

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  4. Astbury and Bell, Nature, 147, 696 (1941).

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BAMFORD, C., HANBY, W. & HAPPEY, F. Solubilities of the αII- and β-Forms of Synthetic Polypeptides: Evidence for an αII–β Transformation in the Amorphous Phase. Nature 166, 829–830 (1950). https://doi.org/10.1038/166829b0

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