The adsorption of the proteins, bovine serum albumin, fibrinogen, avidin and neutravidin (non-glycosylated form of avidin) to a variety of surfaces imposed on thickness shear mode sensors in examined in a flow-injection analysis format. In all cases, adsorption of these moieties was essentially irreversible, although the magnitude of adsorption was dependent on surface free energy and functional group chemistry. Also described is the direct, real-time detection of the binding of peptides to HIV-1 TAR RNA bound on a thickness-shear mode (TSM) sensor surface. The results clearly indicate that responses are discriminatory for two different peptides. In order to provide a theoretical backcloth for the experimental measurements, a new model for the operation of the TSM in liquids is presented.