Protein adsorption from (aqueous) solutions onto a (solid) surface is a common process that takes place at biological interfaces. This phenomenon, that spontaneously occurs, changes the properties of the surface and can induce structural modifications on proteins. Proteins in solution can be easily identified/quantified using classical biochemical methods. However, adsorbed proteins are more difficult to assess since they are always associated with a substrate. The selection of the analytical method depends on the type of substrate used, the amount of adsorbed protein, the type of solution (single protein solution vs. complex biological media), and the type of information that is demanded (quantification of the adsorbed protein, adsorption kinetics, conformation, and orientation of the adsorbed protein). Until now, none of the techniques available are capable by its own to characterize all the protein adsorption process. Therefore, a multitechnique analysis is required. During this chapter, the methodologies to measure human serum albumin to poly(ethylene terephthalate) using the three different techniques, radiolabeling, ellipsometry, and quartz crystal microbalance with dissipation – QCM-D, are described in detail. The specific preparation of polymeric surfaces to be used with each technique is also presented.