Abstract
Voltage-gated cation (e.g. Na+, K+) channels are central to neurological signal transmission. The mechanism of voltage-gating, namely the coupling of conformational changes in the voltage sensing domain (VSD) in response to depolarizing potentials with respect to the resting transmembrane electric potential, to opening the pore domain (PD) resulting in transmembrane ionic current, remains unresolved. We report the direct measurement of changes in the scattering-length density (SLD) profile of the VSD protein, vectorially-oriented within a reconstituted phospholipid bilayer membrane, as a function of the transmembrane electric potential by time-resolved x-ray and neutron interferometry. The changes in the experimental SLD profiles are predicted by molecular dynamics simulations, thus providing an interpretation in terms of the VSD's atomic-level 3-D structure.
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