Characterizing Channelrhodopsin Channel Properties Via Two-Electrode Voltage Clamp and Kinetic Modeling

Channelrhodopsin C1C2: Photocycle kinetics and interactions near the central gate

“…In contrast, the extracellular side expanded by $1 A ˚. In this variant, the fewest number of waters on average (16) entered the transmembrane region of the pore.…”

“…2) in their closed and open states. Electrophysiological studies were used to measure opening and closing rates of the channels, as previously described (16). Atomistic simulations were applied to investigate the network of chemical interactions among key gating residues, as well as pore structure and hydration, to determine how mutations affect those properties (17).…”