Ontology highlight
ABSTRACT:
SUBMITTER: Freites JA
PROVIDER: S-EPMC1635690 | biostudies-literature | 2006 Dec
REPOSITORIES: biostudies-literature
Biophysical journal 20060929 11
Voltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close in response to changes in transmembrane potential. Recent experimental studies suggest that VS domains are independent structural units. This independence is revealed dramatically by a voltage-dependent proton-selective channel (Hv), which has a sequence homologous to the VS domains of voltage-gated potassium channels (Kv). Here we show by means of molecular dynamics simulations that the isolated open-stat ...[more]