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      Conformations and Currents Make the Nerve Signal

      In review


            Little is known about how conformation changes of proteins control biological function. How do the locations reveal themselves as measurable physical properties of the protein?One place these questions can be (mostly) answered is in the proteins that form the voltage activated channels of nerve.

            We calculate conformation currentin Na Vand K V channels in response to a step of voltage. Changing isoleucine of K V channels to threonine of Na V channels speeds responses to voltage, andallows the separation of opening of Na V and K V channels needed to create nerve signals.

            The polarization mechanism we propose is both logically sufficient and logically necessary to account for the difference in speed and the structural movements of voltage sensors. It is sufficient because we reproduce properties of gating current under a realistic range of conditions.It is necessary because the movement of chargeswe calculate must produce the currents we calculate given the universal and exact nature of the Maxwell equations that link charge and current. Our conclusions arise fromthe universal and exact conservation of total current implied by the Maxwell equations.

            Of course, evolution is not logical. It often provides redundant mechanismsbeyond the necessary and sufficient. These mechanisms may provide properties not glimpsed here. These mechanisms may also control the speed of gating and give the gating system biologically and evolutionarily useful properties unknown to us.


            Author and article information

            ScienceOpen Preprints
            15 June 2022
            [1 ] Applied Mathematics, Illinois Institute of Technology; Physiology and Biophysics, Rush University, Chicago IL USA
            [2 ] Department of Chemistry, Biology and Biotechnology, University of Perugia, Via Elce di Sotto 8, 06123 Perugia, Italy
            [3 ] Department of Chemistry, Biology and Biotechnology, University of Perugia, Via Elce di Sotto 8, 06123 Perugia, Italy
            Author notes

            This work has been published open access under Creative Commons Attribution License CC BY 4.0 , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Conditions, terms of use and publishing policy can be found at www.scienceopen.com .

            The datasets generated during and/or analysed during the current study are available from the corresponding author on reasonable request.
            Chemistry,Engineering,Physics,Life sciences
            Brownian Dynamics,Volage Sensitive Channels,Gating Current,; Molecular Dynamics,Conformation changes


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