Voltage Dependent Profile Structures of a Voltage-Gated K+ Channel via Time-Resolved Neutron Interferometry (Biophysical Journal)

Available experimental techniques cannot determine high-resolution 3-D structures of membrane proteins under a transmembrane voltage. Hence, the mechanism by which voltage-gated cation channels couple conformational changes within the four voltage sensor domains, in response to either depolarizing or polarizing transmembrane voltages, to opening or closing of the pore domain`s ion channel remains unresolved. Single membrane specimens, comprised of a phospholipid bilayer containing a vectorially-oriented voltage-gated K+ channel protein at high in-plane density tethered to the surface of an inorganic multilayer substrate, were developed to allow the application of transmembrane voltages in an electrochemical cell.