A quantitative assessment of models for voltage-dependent gating of ion channels.

ABSTRACT: Voltage-gated ion channels open and close, or "gate," in response to changes in membrane potential. The electric field across the membrane-protein complex exerts forces on charged residues driving the channel into different functional conformations as the membrane potential changes. To act with the greatest sensitivity, charged residues must be positioned at key locations within or near the transmembrane region, which requires desolvating charged groups, a process that can be energetically prohibitive. Although there is good agreement on which residues are involved in this process for voltage-activated potassium channels, several different models of the sensor geometry and gating motions have been proposed. Here we incorporate low-resolution structural information about the channel into a

SUBMITTER: Grabe M 

PROVIDER: S-EPMC539724 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature