Based upon our previous work , we generalized the KS theory of protonisation fluctuation by calculating the electrostatic and CR free energy contributions due to anisotropic distribution of dissociable charges on a sphere circumscribed to a protein. This allowed us to implement and solve for the weak-coupling CR boundary condition as well as quadratic fluctuations around it. We show that fluctuations in both the total charge and the total dipole moment depend on the same proton occupancy correlator δq k δq t . As a result, both the capacitance (proportional to the charge fluctuations) as well as the polarizability (proportional to the dipole fluctuations) of the protein depend in a similar fashion on the solution pH through the proton occupancy correlator. This is surprising, as these two lowest multipoles, i.e., monopole and dipole, describe two linearly independent terms in the spherical harmonic expansion of the electrostatic interaction energy; in fact, it is known that their equilibrium values, q and p, show vastly different pH behavior . We also show that the strength of the KS fluctuation interaction in the asymptotic regime of protein-protein separation is modified and depends additively on the capacitance and polarizability of the two interacting proteins. As a consequence, the strength of the KS interaction acquires a strong pH and salt dependence.