Experimental studies have shown the formation of soluble complexes in the pure repulsive Coulombic regime even when the net charges of the protein and the polyelectrolyte have the same sign (De Kruif et al. Curr. Opin. Colloid Interface Sci. 2004, 9, 340; De Vries et al. J. Chem. Phys. 2003, 118, 4649; Grymonpre et al. Biomacromolecules 2001, 2, 422; Hattori et al. Langmuir 2000, 16, 9738). This attractive phenomenon has often been described as "complexation on the wrong side of pI". While one theory assumes the existence of "charged patches" on the protein surface from ion dipole interactions, thus allowing a polyelectrolyte to bind to an oppositely heterogeneous charged protein region, another theoretical view considers the induced-charge interactions to be the dominant factor in these complexations. This-charge regulation mechanism can be described by proton fluctuations resulting from mutual rearrangements of the distributions of the charged groups; due to perturbations of the acid base equilibrium. Using constant-pH Monte Carlo simulations and severall quantitative and visual analysis tools, we investigate the significance of each of these interactions for two whey proteins, alpha-lactalbumin (alpha-LA) and lysozyme (LYZ). Through physical chemistry parameters, free energies of interactions, and the mapping of amino acid pK(a) shifts and polyelectrolyte-trajectories, we show the charge regulation mechanism to be the most,important contributor in protein polyelectrolyte complexation regardless of pH, dipole moment, and protein capacitance in low salt regime.