Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.

ABSTRACT: Available experimental techniques cannot determine high-resolution three-dimensional 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, composed 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. Time-resolved neutron reflectivity experiments, enhan

SUBMITTER: Tronin AY 

PROVIDER: S-EPMC6712512 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature