We calculate communication maps for Photoactive Yellow Protein (PYP) from the purple phototropic eubacterium Halorhodospira halophile and use them to elucidate energy transfer pathways from the chromophore through the rest of the protein in the ground and excited state. The calculations reveal that in PYP excess energy from the chromophore flows mainly to regions of the surrounding residues that hydrogen bond to the chromophore. In addition, quantum mechanics/molecular mechanics and molecular dynamics (MD) simulations of the dielectric response of the protein and solvent environment due to charge rearrangement on the chromophore following photoexcitation are also presented, with both approaches yielding similar time constants for the response. Results of MD simulations indicate that the residues hydrogen bonding to the chromophore make the largest contribution to the response.