Voltage and Time Dependence of Amphotericin B Channel Activity in Lipidic Membranes

Abstract

and fluorophore labeling of the human Kir2.1 channel, which are reconstituted into liposomes of various lipid composition. We have measured PIP2dependent FRET changes at numerous sites, which indicate structural movements of the intracellular domain of Kir2.1 upon PIP2 binding. This work specifically investigates how movements of the slide helix contribute to activation of the channel. Further efforts will help to define the molecular details of bulk anionic lipid and PIP2-dependent structural dynamics of Kir2.1 and help to understand more generally how lipid-protein interactions regulate membrane protein function.