The development of electrostatic parameters for additive biomolecular force fields is problematic owing to the fundamentally different environments in which the atomic partial charges are first derived (generally by gas-phase QM calculations upon individual amino acids or fragments) and then applied (condensed-phase simulations of large macromolecular complexes, including water, ions and other solutes). The Amber and Charmm force field families, like many others, have compensated for the effects of transferring parameters to the condensed phase by fitting partial charges that are intrinsically overpolarized. This approximation is ultimately inadequate, and recognition of this fact has contributed to the drive to develop accurate explicitly polarizable models. Nevertheless, parametrization processes for additive models are generally intended to recreate intermolecular energetics (determined by the electrostatic potential at a given site) and forces (determined by the electric field) as accurately as possible. However our results for CypA suggest that the intrinsic overpolarization of atomic partial charges is insufficient to recreate the effects of induction upon intramolecular electric fields, and that this issue may be generalizable to multiple force field families. The polarization model in AMOEBA is both a more accurate electrostatic model overall, with reduced random error and improved correlation to DFT fields, and does not show a sizable systematic error in electric fields, with a near unity slope in comparison to DFT (Fig ).