One key for the successful integration of implants into the human body is the control of protein adsorption by adjusting the surface properties at different length scales. This is particularly important for titanium oxide, one of the most common biomedical interfaces. As for titania (TiO2) the interface is largely defined by its crystal surface structure, it is crucial to understand how the surface crystallinity affects the structure, properties and function of protein layers mediating subsequent biological reactions. For rutile TiO2 we demonstrate that the conformation and relative amount of human plasma fibrinogen (HPF) and the structure of adsorbed HPF layers depend on the crystal surface nanostructure by employing thermally etched multi-faceted TiO2 surfaces. Thermal etching of polycrystalline TiO2 facilitates a nanoscale crystal faceting and, thus, the creation of different surface nanostructures on a single specimen surface. Atomic force microscopy shows that HPF arranges into networks and thin globular layers on flat and irregular crystal grain surfaces, respectively. On a third, faceted category we observed an alternating conformation of HPF on neighboring facets. The bulk grain orientation obtained from electron backscatter diffraction and thermodynamic mechanisms of surface reconstruction during thermal etching suggest that the grain and facet surface-specific arrangement and relative amount of adsorbed proteins depend on the associated free crystal surface energy. The implications for potentially favorable TiO2 crystal facets regarding the inflammatory response and hemostasis are discussed with a view to the advanced surface design of future implants.