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Biophys J, August 2001, p. 827-837, Vol. 81, No. 2
Department of Medical Biophysics, Göteborg University, 40530 Göteborg, Sweden
The formation kinetics of gramicidin A channels in lipid
bilayer membranes has been characterized as a function of voltage for
different solution conditions and membrane composition. The frequency
of channel events was measured during the application of voltage ramps
and counted in given intervals, a procedure that eliminated the effects
of drift in gramicidin concentration. The formation rate was found to
increase strongly with voltages up to ~50 mV and then to level off
slightly. The shape of the voltage dependence was independent of lipid
solvent and ramp speed but differed for different ions and different
solution concentrations. This suggested an ion occupancy effect on the
formation rate that was further supported by the fact that the minimum
of the formation rate was shifted toward the equilibrium potential in
asymmetric solution concentrations. The effects are explained in terms
of a model that contains two contributions to the voltage dependence, a
voltage-dependent ion binding to the monomers and a polarization of
monomers by the applied electric field and by the occupied ions. The
theory is found to give a good fit to experimental data.
Biophys J, August 2001, p. 827-837, Vol. 81, No. 2
© 2001 by the Biophysical Society 0006-3495/01/08/827/11 $2.00
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