Hydration water on the surface of a protein is thought to mediate the thermodynamics of protein-ligand interactions. For hydration water to play a role beyond modulating global protein solubility or stability, the thermodynamic properties of hydration water must reflect on the properties of the heterogeneous protein surface and thus spatially vary over the protein surface. A potent read-out of local variations in thermodynamic properties of hydration water is its equilibrium dynamics spanning picosecond to nanosecond time scales. In this study, we employ Overhauser dynamic nuclear polarization (ODNP) to probe the equilibrium hydration water dynamics at select sites on the surface of Chemotaxis Y (CheY) in dilute solution. ODNP reports on site-specific hydration water dynamics within 5-10 Å of a label tethered to the biomolecular surface on two separate time scales of motion, corresponding to diffusive water (DW) and protein-water coupled motions, referred to as bound water (BW). We find DW dynamics to be highly heterogeneous across the surface of CheY. We identify a significant correlation between DW dynamics and the local hydropathy of the CheY protein surface, empirically determined by molecular dynamics (MD) simulations, and find the more hydrophobic sites to be hydrated with slower diffusing water. Furthermore, we compare the hydration water dynamics on different polypeptides and liposome surfaces and find the DW dynamics on globular proteins to be significantly more heterogeneous than on intrinsically disordered proteins (IDPs), peptides, and liposomes. The heterogeneity in the hydration water dynamics suggests that structured proteins have the capacity to encode information into the surrounding hydration shell.