Aggregation of Tau, a soluble intrinsically disordered protein, into insoluble protein aggregates forms a defining hallmark of a sub-set of neurodegenerative diseases together referred to as tauopathies. In vivo, large surface areas encountered in the cellular environment has been suggested to play a governing role in the aggregation process. In this work, a quartz crystal microbalance with dissipation (QCM-D) is used to monitor the kinetics of protein adsorption to hydrophobic and hydrophilic solid surfaces as model systems representing surfaces in the crowded cellular environment. Further, a wild type and an assembly incompetent tau protein are studied to monitor the role of biochemistry on the kinetics of protein adsorption to different surfaces. The kinetics of adsorption are modelled using COMSOL Multiphysics simulation software, and found to fit the experimental data accurately using multi-step adsorption models that include adsorption as well as conformational changes upon adsorption to the surfaces. Finally, atomic force microscopy (AFM) images are used to confirm that in addition to protein biochemistry, the dynamics of protein adsorption, particularly restructuring of the proteins upon adsorption to different surfaces, is an important first step that controls the presence of protein aggregates on the different surfaces. Our results together suggest that while the adsorption of the tau proteins to a hydrophobic surface is modulated by the hydrophobicity of the microtubule binding region of the protein, the tendency to aggregate at any surface is also modulated by the kinetics of protein adsorption and restructuring at that surface.