Abstract
A theory for calculating the proton flux through the influenza virus M2 channel is tested here against an extensive set of conductance data. The flux is determined by the rate constants for binding to the His(37) tetrad from the two sides of the membrane and the corresponding unbinding rate constants. The rate constants are calculated by explicitly treating the structure and dynamics of the protein. Important features revealed by previous studies, such as a gating role for Val(27) at the entrance to the channel pore, and channel activation by viral exterior pH, are incorporated in this theory. This study demonstrates that the conductance function of the M2 proton channel can now be quantitatively rationalized by the structure and dynamics of the protein.