ArticleBiophysics and physicobiology2025
FTIR study of the wild-type and mutant proteins of a viral rhodopsin, OLPVR1.
Article in Biophysics and physicobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
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3 authors.
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Abstract
OLPVR1 is a viral channelrhodopsin found in giant viruses, which can be a useful optogenetic tool for calcium-regulated cell functions. Determination of the open-state structure leads to one of the best understood channelrhodopsins. Recent FTIR spectroscopy of OLPVR1 reported unique structures in the resting and photoisomerized states at 77 K. Here we attempted to obtain difference FTIR spectra of mutants in OLPVR1, where we focused six key residues, S11, E44, E51, D76, D200, and N205. We prepared S11T, E51D, E51Q, N205Q, E44Q, D76N, and D200N, to which spectroscopic analysis was applied. From the λ
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