The principle of gating charge movement in a voltage-dependent K(super +) channel

Article Abstract:

KvAP channels were reconstituted into planar lipid membranes and studied using monoclonal Fab fragments, a voltage-sensor toxin. It was concluded that the voltage-sensor paddles operate somewhat like hydrophobic cations attached to levers, enabling the membrane electric field to open and close the pore.

Membrane fusion, Cations, Hydrophobic effect

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X-ray structure of a voltage-dependent K(super +) channel

Article Abstract:

The structure of KvAP, a voltage-dependent K(super +) channel from Aeropyrum pernix is presented. A crystal structure of the full-length channel at a resolution of 3.2 A, and of the isolated voltage-sensor domain at 1.9A, is determined, both in complex with monoclonal Fab fragments.

Crystals, Crystal structure, Ions, Action potentials (Electrophysiology), Action potentials

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Atomic structure of a voltage-dependent [K.sup.+] channel in a lipid membrane-like environment

Article Abstract:

The article explains the atomic structure of a chimaeric voltage-dependent [K.sup.+] (Kv) channel surrounded by a lipid membrane-like environment. These channels are widely used for the repolarization of the action potential in neurons and muscle.

Current-Carrying Wiring Device Manufacturing, Current-carrying wiring devices, Voltage Regulators (Customer Eqp), Physiological aspects, Muscles, Potassium channels, Neurons, Voltage regulators, Electric current regulators

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