Optical Rotation of Irradiated Rhodopsin Solution

IT has been suggested from spectroscopic observations of rhodopsin 1–3 that the photoisomerization of chromophore—11- cis to all- trans retinal—must be followed by a conformational change in the protein moiety of the rhodopsin molecule, which is considered to play an important part in the initiation...

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Bibliographic Details
Published in:Nature (London) 1966-07, Vol.211 (5045), p.197-198
Main Authors: KITO, YUJI, TAKEZAKI, MASAMI
Format: Article
Language:English
Subjects:
Chemical Phenomena
Chemistry, Physical
Humanities and Social Sciences
letter
multidisciplinary
Radiation Effects
Retinal Pigments
Science
Science (multidisciplinary)
Solutions
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Summary:IT has been suggested from spectroscopic observations of rhodopsin 1–3 that the photoisomerization of chromophore—11- cis to all- trans retinal—must be followed by a conformational change in the protein moiety of the rhodopsin molecule, which is considered to play an important part in the initiation of visual impulses. Such a conformational change in the protein should be determined by direct measurement of the optical rotation, as this is believed to be closely related to the conformation of the protein 4–6 . The purpose of the present investigation was to determine how far the rotatory polarization of rhodopsin solution changes in response to bleaching by light.
ISSN:0028-0836
1476-4687
DOI:10.1038/211197a0