Given this interest, here we test the ability of biomolecular force fields to reproduce the electric fields inside a whole protein and its associated solvent and ionic environment, using the peptidyl-prolyl isomerase cyclophilin A (CypA) as a model system. We choose to evaluate the accuracy of the AMOEBA polarizable force field, as it has recently been promisingly used in proof-of-concept work for enzyme design. Although ultimately successful in redesigning active site interactions, the additional computational cost of AMOEBA has prevented lengthy studies of active site dynamics, and there has been little assessment so far of the physical accuracy of AMOEBA electric fields within the folded protein environment over typical simulation timescales.