The DC gate in Channelrhodopsin-2: crucial hydrogen bonding interaction between C128 and D156.

@article{Nack2010TheDG,
  title={The DC gate in Channelrhodopsin-2: crucial hydrogen bonding interaction between C128 and D156.},
  author={Melanie Nack and Ionela Radu and Michael Gossing and Christian Bamann and Ernst Bamberg and Gabriele Fischer von Mollard and Joachim Heberle},
  journal={Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology},
  year={2010},
  volume={9 2},
  pages={194-8}
}
The light-gated cation channel Channelrhodopsin-2 (ChR2), a retinylidene protein found in the eye-spot of Chlamydomonas reinhardtii, became an optogenetic tool to trigger neurophysiological responses by light and, thus, revolutionized spatio-temporal studies of such processes. The reaction mechanism still remains elusive but recent vibrational spectroscopic experiments started to resolve details of the associated structural changes during the photocycle. Large alterations in the polypeptide… CONTINUE READING

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