id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_hwxx5didljd2lk5lo4bevhxtza	Brian Urbani	Gating Interactions between the Cytoplasmic T1 Domain and Pore of a Kv Channel	2013	1	.pdf	application/pdf	1657	96	54	Voltage-activated potassium (Kv) channels open an intracellular gate in response to changes in transmembrane voltage, allowing K N-terminus of the protein acting as a blocking particle, binding at the intracellular cavity of the channel and physically obstructing the permeation pathway. results suggest that despite being tethered to a particular subunit, the single inactivation particle has sufficient freedom to interact with position 470 of each from the solution; from the gate it repels an ion in the channel pore cavity into Water Structure at the Potassium Channel Gate: The Importance of the Gating Interactions between the Cytoplasmic T1 Domain and Pore of a Kv Channel Is the Activation Gate Closed in Kv Channel Closed-State Inactivation? Is the Activation Gate Closed in Kv Channel Closed-State Inactivation? Water Structure at the Potassium Channel Gate: The Importance of the Prolines in the PVPV Sequence, as Shown by Computation ...	./cache/work_hwxx5didljd2lk5lo4bevhxtza.pdf	./txt/work_hwxx5didljd2lk5lo4bevhxtza.txt