Publications by authors named "Michael B Partenskii"

The coupling of electric fields and charges with membrane-water interfacial fluctuations affects membrane electroporation, ionic conductance, and voltage gating. A modified continuum model is introduced to study charge interaction with membrane-water interfacial fluctuations in multidielectric environments. By surrounding a point charge with a low dielectric sphere, the linear Poisson-Boltzmann equation is directly solved by calculating the reaction field potential via a method that eliminates singularity contributions.

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Negative capacitance (NC), predicted by various electrical double layer (EDL) theories, is critically reviewed. Physically possible for individual components of the EDL, the compact or diffuse layer, it is strictly prohibited for the whole EDL or for an electrochemical cell with two electrodes. However, NC is allowed for the artificial conditions of sigma control, where an EDL is described by the equilibrium electric response of electrolyte to a field of fixed, and typically uniform, surface charge-density distributions, sigma.

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Theoretical studies of electrical double layers typically consider the response of ionic conductors to the field of uniform charge-density distributions sigma ("sigma -control"). Many such analyses predict apparent anomalies of differential capacitance, C , including divergences and negative values. To clarify misconceptions regarding these predictions, we critically reexamine some theoretical approaches dealing with the admissible sign of C .

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Membrane-mediated interaction between membrane-spanning peptides or protein segments plays an important role in their function and stability. Our rigorous "coupled harmonic oscillators" representation is extended to account for the complex boundary conditions permitting anisotropic relaxation of the membrane slope along the contours of the inclusions. Using this representation and applying a highly efficient finite-difference algorithm, we have analyzed the membrane-mediated interaction triggered by deformation of the hydrophobic tails of lipid molecules to match the lipophilic exterior of the inserted peptide.

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