  In order to find the exact form of the electrostatic interaction between two
proteins with dissociable charge groups in aqueous solution, we have studied a
model system composed of two macroscopic surfaces with charge dissociation
sites immersed in a counterion-only ionic solution. Field-theoretic
representation of the grand canonical partition function is derived and
evaluated within the mean-field approximation, giving the Poisson-Boltzmann
theory with the Ninham-Parsegian boundary condition. Gaussian fluctuations
around the mean-field are then analyzed in the lowest order correction that we
calculate analytically and exactly, using the path integral representation for
the partition function of a harmonic oscillator with time-dependent frequency.
The first order (one loop) free energy correction gives the interaction free
energy that reduces to the zero-frequency van der Waals form in the appropriate
limit but in general gives rise to a mono-polar fluctuation term due to charge
fluctuation at the dissociation sites. Our formulation opens up the possibility
to investigate the Kirkwood-Shumaker interaction in more general contexts where
their original derivation fails.
