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Date uploaded: April 21, 2023

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Ultrafast molecular animation of proteins involved in vision -How we sense light in dim light

Press Release 20230323

Summary

An international collaborative research group consisting of Sou Iwata (RIKEN SPring-8 Center and Kyoto University), Eriko Nango (Tohoku University and RIKEN SPring-8 Center), and Kensuke Tono (Japan Synchrotron Radiation Research Institute) has successfully captured moving images of the ultrafast changes upon light stimulation in rhodopsin, a protein involved in vision, clearly showing the atomic movements from 1 picosecond (one trillionth of a second) to 100 picoseconds using an X-ray free electron laser (XFEL).

These research results are expected to lead not only to a better understanding of the mechanisms of human vision, but also to important insights into the activation mechanism of G protein-coupled receptors, which are important drug targets.

Rhodopsin is a membrane protein found in the retina of the eye that contains a conjugated aldehyde called retinal to catch light. Rhodopsin is highly sensitive to light and thus plays a role in seeing objects in dimly lit environments (night vision). When exposed to light, rhodopsin undergoes a structural change that is transmitted as a signal into the cell, ultimately enabling it to "see" objects. However, the details of the retinal changes inside rhodopsin were unknown.

In this study, the international research group succeeded in capturing atomic-level moving images of rhodopsin changes induced by light, and elucidated the mechanism at the early stage of vision.

This research was published online in the scientific journal Nature prior to its publication (March 22: March 23, Japan time)



  • (The original press release is in Japanese)

    https://www.tohoku.ac.jp/japanese/2023/03/press20230323-01-vision.html http://www2.tagen.tohoku.ac.jp/lab/news_press/20230323/



    Publication details

    Title:

    Ultrafast structural changes direct the first molecular events of vision

    Authors

    Thomas Gruhl1, Tobias Weinert, Matthew J. Rodrigues, Christopher J. Milne ,Giorgia Ortolani, Karol Nass, Eriko Nango, Saumik Sen, Philip J. M. Johnson, Claudio Cirelli, Antonia Furrer, Sandra Mous, Petr Skopintsev, Daniel James, Florian Dworkowski, Petra Båth, Demet Kekilli, Dmitry Ozerov, Rie Tanaka, Hannah Glover, Camila Bacellar, Steffen Brünle1, Cecilia M. Casadei, Azeglio D. Diethelm, Dardan Gashi, Guillaume Gotthard1, Ramon Guixà-González, Yasumasa Joti, Victoria Kabanova, Gregor Knopp, Elena Lesca1, Pikyee Ma, Isabelle Martiel, Jonas Mühle, Shigeki Owada, Filip Pamula1, Daniel Sarabi, Oliver Tejero, Ching-Ju Tsai, Niranjan Varma, Anna Wach, Sébastien Boutet, Kensuke Tono, Przemyslaw Nogly, Xavier Deupi, So Iwata, Richard Neutze, Jörg Standfuss1, Gebhard Schertler, Valerie Panneels

    Journal

    Nature Vol 615, 939-944, 2023

    DOI

    10.1038/s41586-023-05863-6





    Contact

    (Research)
    Professor Eriko NANGO
    E-mail: eriko.nango.c4 [at]tohoku.ac.jp
    Please replace [at] with "@" in the email address.

    (Press)
    E-mail: press.tagen [at]grp.tohoku.ac.jp
    Please replace [at] with "@" in the email address.