The adsorption of mussel adhesive protein (MAP) from the marine mussel Mytilus edulis has been investigated on polystyrene (PS) and poly(octadecyl methacrylate) (POMA) surfaces using angle dependent X-ray photoelectron spectroscopy (XPS) and atomic force microscopy(AFM). AFM images previously published in the dehydrated state using contact mode are compared with images acquired in the hydrated state using fluid Tapping Mode to assess the contribution that hydration has on the architecture of the adsorbed proteins. To further characterize the adsorbed protein layer XPS analysis was performed at liquid nitrogen (LN2) temperature without dehydrating the samples and at room temperature after the surfaces were dehydrated. The differences observed upon dehydration can be attributed to the strength of the interactions between MAP and the two surfaces. The AFM and XPS data indicate that adsorbed MAP is stabilized on the surface of the PS through interactions that prevent the protein layer from being disrupted upon dehydration. The adsorbed MAP on the POMA surface is representative of a loosely bound protein layer that becomes highly perturbed upon dehydration.