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

IT is well known that the α-helix configuration of Pauling and Corey 1 is associated with a carbonyl stretching mode in the neighbourhood of 1,652–1,655 cm. −1 in films of simple enantiomorphic polypeptides 2,3 . Since this frequency is also found in the infra-red spectra of films prepared from a nu...

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Bibliographic Details
Published in:Nature (London) 1957-12, Vol.180 (4598), p.1340-1341
Main Authors: ELLIOTT, A, HANBY, W. E, MALCOLM, B. R
Format: Article
Language:English
Subjects:
Humanities and Social Sciences
letter
multidisciplinary
Science
Science (multidisciplinary)
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Summary:IT is well known that the α-helix configuration of Pauling and Corey 1 is associated with a carbonyl stretching mode in the neighbourhood of 1,652–1,655 cm. −1 in films of simple enantiomorphic polypeptides 2,3 . Since this frequency is also found in the infra-red spectra of films prepared from a number of native proteins 4–6 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 fibroin 7 , 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/1801340b0