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Light-sensitive proteins called rhodopsins in the vertebrate eye initiate the cellular processes of vision. Leading-edge crystallography experiments have revealed the molecular mechanism by which light activates these proteins.
Marius Schmidt is in the Department of Physics, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, USA. Emina A. Stojković is in the Department of Biology, Northeastern Illinois University, Chicago, Illinois 60625, USA. Most vertebrate animals depend on vision to navigate their environment and avoid predators. In the vertebrate eye, light is converted into electrical signals by a receptor protein known as rhodopsin, which spans the membranes of rod cells in the retina; the electrical signals are then processed in the brain to generate a mental image. The 'master switch' that responds to light and activates rhodopsin is a pigment called retinal1,2 — an organic cofactor and derivative of vitamin A. Writing in Nature, Gruhl et al.3 report ultrafast, time-resolved crystallography experiments that show how this switch is flipped, finally revealing the molecular mechanism of rhodopsin activation. Access Nature and 54 other Nature Portfolio journals Get Nature+, our best-value online-access subscription $29.99 / 30 days cancel any time Subscribe to this journal Receive 51 print issues and online access $199.00 per year only $3.90 per issue Rent or buy this article Prices vary by article type from$1.95 to$39.95 Prices may be subject to local taxes which are calculated during checkout Nature 615, 802-803 (2023) doi: https://doi.org/10.1038/d41586-023-00504-4 Ernst, O. P. et al. Chem. Rev. 114, 126-163 (2014). Article
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Download references The authors declare no competing interests.
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