Temperature dependence of gramicidin channel conductance

The gramicidin channel is the smallest known biological ion channel, and it exhibits cation selectivity. Recently, Dr. John Cuppoletti's group at the University of Cincinnati has shown that the gramicidin channel can function at high temperatures with significant currents. This finding may have implications for fuel cell technologies. In order to explore the effect of temperature on channel conductance, we examined the gramicidin system at 300K, 330K, and 360K by computer simulation. Two forms of gramicidin, the head-to-head helical dimer and the intertwined double helix, were examined. Both the decrease of the free energy barrier and the increase of the diffusion of potassium ions inside the gramicidin channel at high temperatures imply an increase of current. We found that higher temperatures also affect the lifetime of hydrogen bonds, the distribution of the bending angle, the distribution of the distance between dimers, and the size of the pore radius for the helical dimer structure. These finding may be related to the gating of the gramicidin channel.