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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ELLIOTT, A., HANBY, W. & MALCOLM, B. Optical Rotation and Infra-Red Spectra of some Polypeptide and Protein Films. Nature 180, 1340–1341 (1957). https://doi.org/10.1038/1801340b0
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