We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Optical Rotation and Infra-Red Spectra of some Polypeptide and Protein Films.
- Authors
ELLIOTT, A.; HANBY, W. E.; MALCOLM, B. R.
- Abstract
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.
- Publication
Nature, 1957, Vol 180, Issue 4598, p1340
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/1801340b0