By Hugo O. Villar (Eds.)
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Additional info for Advances in Computational Biology
If either of the sites are 5 or 6, then /pj = <». The important interaction for channel formation is the highly anisotropic interaction between the sides of two proteins which are allowed to share the same bond. This is only advantageous when one side is (1,2) of the first protein and the second side is (3,4) of the second protein with comer 1 on the same site as comer 4, as shown in Figure 3(b). The interaction in this case is attractive and given by -J^iThe outer sites (comers) of proteins interact anisotropically with the uniform lipid background except when more than one such site occupies the same site on the lattice.
Only contact interactions, either between two neighboring proteins or between a protein and the surrounding lipids, are taken into consideration. The interactions between proteins are assumed to be highly anisotropic as follows. Let us label the comers (lattice sites) on each protein hexagon from 1 to 6 as shown in Figure 3(a). The comers of two neighboring hexagons occupying the same site interact with a mutual repulsion, 7pj. If either of the sites are 5 or 6, then /pj = <». The important interaction for channel formation is the highly anisotropic interaction between the sides of two proteins which are allowed to share the same bond.
For F^ = 4 x 10"^^erg/A, the height of the barrier does not depend on system size to within calculational error, indicating that the transition for this parameter value is almost at a critical point. The temperature and size dependence of the specific heat are shown in Figure 6(a) for F^ = 5x10"^Srg/A corresponding to a first-order transition. As the system size increases, the peak height of C(T) increases while the width of the peaks decreases. The peak height scales as expected for a first-order transition, Eq.