The protein or membrane environment could respond to an external field in a number of different ways. Field induced dipoles, reorientation of permanent dipoles, protonation and deprotonation of protein residues, larger scale reorganization of ionized side-chains and water molecules, both within the interior and on the surface of the protein, are all examples of how complicated the assignment of permittivity is. In MD simulations, where all the charges, dipoles, and field induced atomic dipoles are treated explicitly then it is suggested that a dielectric value of 1 is appropriate. However, in reduced-particle ion simulation programs, such as ours, where the protein, membrane, and water are continuum backgrounds and treated implicitly, and on top of that, the ion motion takes place on the same time-scale as the protein’s response to its presence, it is very difficult to assign the dielectric coefficients. In fact, changing the dielectric coefficients could easily alter the channel characteristics, such as ion permeation and selectivity The assignment of dielectric coefficient for water is another key issue. The water molecules inside ion channels could be very ordered due to tapered size of the pore, which is often lined with highly charged residues, or hydrogen bond formation between water molecules and protein. As a result, the dielectric constant of water inside an ion channel could be quite different from the value under bulk conditions. To make the matter even more complicated, the dielectric coefficients of water inside nanopores is not necessarily an isotropic scalar value, but an anisotropic tensor having different values in different directions.