Abstract
Rhodopsin is a seven-helical transmembrane protein with a retinal chromophore covalently bound to a conserved lysine in helix G via a retinal protonated Schiff base (RPSB). Microbial rhodopsins absorb light through chromophore and play a fundamental role in optogenetics. Numerous microbial rhodopsins have been discovered, contributing to diverse functions and colors. Solid-state NMR spectroscopy has been instrumental in elucidating the conformation of chromophores and the three-dimensional structure of microbial rhodopsins. This review focuses on the 15N chemical shift values of RPSB and summarizes recent progress in the field. We displayed the correlation between the 15N isotropic chemical shift values of RPSB and the maximum absorption wavelength of rhodopsin using solid-state NMR spectroscopy.
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