Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.

ABSTRACT: A variety of experiments suggest that membrane proteins are important targets of anesthetic molecules, and that ion channels interact differently with anesthetics in their open and closed conformations. The availability of an open and a closed structural model for the KirBac1.1 potassium channel has made it possible to perform a comparative analysis of the interactions of anesthetics with the same channel in its open and closed states. To this end, all-atom molecular dynamics simulations supplemented by normal mode analysis have been employed to probe the interactions of the inhalational anesthetic halothane with both an open and closed conformer of KirBac1.1 embedded in a lipid bilayer. Normal mode analysis on the closed and open channel, in the presence and absence of halothane, reveals

SUBMITTER: Vemparala S 

PROVIDER: S-EPMC2480689 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature