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Inside Cover: Light‐Induced Movement of the Transmembrane Helix B in Channelrhodopsin‐2 (Angew. Chem. Int. Ed. 37/2013)
Author(s) -
Sattig Thomas,
Rickert Christian,
Bamberg Ernst,
Steinhoff HeinzJürgen,
Bamann Christian
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201305677
Subject(s) - chemistry , transmembrane domain , helix (gastropod) , transmembrane protein , isomerization , channelrhodopsin , biophysics , chromophore , crystallography , membrane , optogenetics , photochemistry , biochemistry , neuroscience , biology , receptor , catalysis , ecology , snail
Upon light activation of channelrhodopsin‐2 the isomerization of the retinal chromophore triggers a sequence of structural changes finally emerging in an outward movement of the transmembrane helix B. In their Communication on page 9705 ff. , C. Bamann et al. show that this movement could be linked to the transition from the closed to the open state that allows the permeation of cations through the light‐gated cation channel.