Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating
Channelrhodopsin
DOI:
10.1073/pnas.1219502110
Publication Date:
2013-03-19T07:06:17Z
AUTHORS (10)
ABSTRACT
Significance It was always a dream to control cells and living animals by light. Discovery of channelrhodopsin turned the into reality because this light-activated cation channel is able elicit action potentials with unprecedented spatial temporal resolution. To unravel underlying molecular mechanism, we have applied time-resolved IR spectroscopy, suggest how observed proton transfer protein conformational changes lead opening channel. Our results will not only contribute rational design variants improved properties, but also help decipher sequence in gating ion channels.
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