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- W2001063191 abstract "The retinal proteins Channelrhodopsin-1 and −2 (ChR-1 and −2) from Chlamydomonas reinhardtii, which were first described as light-gated ion channels by Nagel et al. in 2002 and 2003, emerged in the last few years as advantageous tools. Since they open up rapidly after absorption of a photon and permeate ions like sodium or calcium, Channelrhodopsins are already used for non-invasive excitation of excitable cells in culture as well as in living tissue. Together with other retinal proteins they share a 7-transmembrane helix motif where the retinal chromophore is covalently linked to the protein via a protonated Schiff base. Recent investigations by Bamann et al. (2008) predicted a photocycle with at least 4 photointermediates, all coupled to the channel function. But little is known about the mechanism that infers the properties of the ion channel or the channel pore, especially the different permeability coefficients between a series of cations and the strong inward-rectifying behaviour of the photocurrents is not fully understood. Here we present a detailed functional characterisation by patch-clamp measurements on HEK293 cells stably expressing Channelrhodopsins. We could show that the inward rectifying properties are associated with the availability of cations and therefore predict cation binding to the protein. These results are discussed in relation to the hypothetical structure of the Channelrhodopsin and a putative cation binding site." @default.
- W2001063191 created "2016-06-24" @default.
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- W2001063191 date "2009-02-01" @default.
- W2001063191 modified "2023-09-26" @default.
- W2001063191 title "Functional investigation of the light-gated Channelrhodopsin" @default.
- W2001063191 doi "https://doi.org/10.1016/j.bpj.2008.12.3546" @default.
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