The binding affinities of polyanions for bovine serum albumin in NaCl solutions from I ) 0.01-0.6 M, were evaluated on the basis of the pH at the point of incipient binding, converting each such pH c value into a critical protein charge Z c . Analogous values of critical charge for mixed micelles were obtained as the cationic surfactant mole fraction Y c . The data were well fitted as Y c or Z c ) KI a , and values of K and a were considered as a function of normalized polymer charge densities (τ), charge mobility, and chain stiffness. Binding increased with chain flexibility and charge mobility, as expected from simulations and theory. Complex effects of τ were related to intrapolyanion repulsions within micelle-bound loops (seen in the simulations) or negative protein domainpolyanion repulsions. The linearity of Z c with I at I < 0.3 M was explained by using protein electrostatic images, showing that Z c at I < 0.3 M depends on a single positive "patch"; the appearance of multiple positive domains I > 0.3 M (lower pH c ) disrupts this simple behavior.