Calculation of deformation energies and conformations in lipid membranes containing gramicidin channels. |
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| Authors: | P Helfrich and E Jakobsson |
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| Affiliation: | Department of Chemistry, University of Illinois, Urbana 61801. |
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| Abstract: | In this paper we calculate surface conformation and deformation free energy associated with the incorporation of gramicidin channels into phospholipid bilayer membranes. Two types of membranes are considered. One is a relatively thin solvent-free membrane. The other is a thicker solvent-containing membrane. We follow the approach used for the thin membrane case by Huang (1986) in that we use smectic liquid crystal theory to evaluate the free energy associated with distorting the membrane to other than a flat configuration. Our approach is different from Huang, however, in two ways. One is that we include a term for surface tension, which Huang did not. The second is that one of our four boundary conditions for solving the fourth-order differential equation describing the free energy of the surface is different from Huang's. The details of the difference are described in the text. Our results confirm that for thin membranes Huang's neglect of surface tension is appropriate. However, the precise geometrical form that we calculate for the surface of the thin membrane in the region of the gramicidin channel is somewhat different from his. For thicker membranes that have to deform to a greater extent to accommodate the channel, we find that the contribution of surface tension to the total energy in the deformed surface is significant. Computed results for the shape of the deformed surface, the total energy in the deformed surface, and the contributions of different components to the total energy, are presented for the two types of membranes considered. These results may be significant for understanding the mechanisms of dimer formation and breakup, and the access resistance for ions entering gramicidin channels. |
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