Letter | Published:

Optical Rotation and Infra-Red Spectra of some Polypeptide and Protein Films

Naturevolume 180pages13401341 (1957) | Download Citation



IT is well known that the α-helix configuration of Pauling and Corey1 is associated with a carbonyl stretching mode in the neighbourhood of 1,652–1,655 cm.−1 in films of simple enantiomorphic polypeptides2,3. Since this frequency is also found in the infra-red spectra of films prepared from a number of native proteins4–6 it is of interest to know whether other configurations besides the α-helix are associated with it, for some X-ray diffraction photographs of fibrous proteins suggest a mixture of crystalline and amorphous forms. In the case of water-soluble films of Bombyx mori silk fibroin7, a completely amorphous X-ray diffraction pattern can be obtained, along with a carbonyl band in the infra-red spectrum at 1,660 cm.−1. It is difficult to think that an α-helix arrangement would not produce sufficient order to reveal the characteristic intensity diffraction pattern of this helix.

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    Yang, J. T., and Doty, P., J. Amer. Chem. Soc., 79, 761 (1957).

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  1. Courtaulds, Ltd., Research Laboratory, Lower Cookham Road, Maidenhead

    • A. ELLIOTT
    • , W. E. HANBY
    •  & B. R. MALCOLM


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