English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Time-Resolved EPR Spectroscopy of Channelrhodopsin-2 Helix B Movements

MPS-Authors
/persons/resource/persons137591

Bamann,  Christian       
Emeritusgroup Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

s00723-023-01612-0-1.pdf
(Any fulltext), 2MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Schumacher, M., Bamann, C., & Steinhoff, H.-J. (2024). Time-Resolved EPR Spectroscopy of Channelrhodopsin-2 Helix B Movements. Applied Magnetic Resonance, 55, 207-218. doi:10.1007/s00723-023-01612-0.


Cite as: https://hdl.handle.net/21.11116/0000-000E-837C-3
Abstract
The light-gated dimeric cation channel channelrhodopsin-2 (ChR2) is one of the most important optogenetic tools. Upon light activation ChR2 undergoes conformational changes, the most prominent ones include a movement of transmembrane helix B. In the present work, we apply time resolved continuous wave EPR spectroscopy to follow spectral changes of a spin label bound to position C79 located in helix B. We observed an increase of the motional freedom of the spin label side chain in illuminated ChR2. The recovery of the underlying light-induced conformational change in the dark is correlated with the recovery of the P480 state of ChR2. The observed conformational changes might be thus key elements responsible for desensitizing the channel for cation conduction.