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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)