Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt D
PROVIDER: S-EPMC2614752 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Schmidt Daniel D MacKinnon Roderick R
Proceedings of the National Academy of Sciences of the United States of America 20081202 49
Voltage-dependent K(+) (Kv) channels underlie action potentials through gating conformational changes that are driven by membrane voltage. In this study of the paddle chimera Kv channel, we demonstrate that the rate of channel opening, the voltage dependence of the open probability, and the maximum achievable open probability depend on the lipid membrane environment. The activity of the voltage sensor toxin VsTx1, which interferes with voltage-dependent gating by partitioning into the membrane a ...[more]