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The introduction in 1990 of a new biosensor technology based on surface plasmon resonance has greatly simplified the measurement of binding interactions in biology. This new technology known as biomolecular interaction analysis makes it possible to visualize the binding process as a function of time by following the increase in refractive index that occurs when one of the interacting partners binds to its ligand immobilized on the surface of a sensor chip. None of the reactants needs to be labelled, which avoids the artefactual changes in binding properties that often result when the molecules are labelled. Biosensor instruments are well-suited for the rapid mapping of viral epitopes and for identifying which combinations of capturing and detector Mabs will give the best results in sandwich assays. Biosensor binding data are also useful for selecting peptides to be used in diagnostic solid-phase immunoassays. Very small changes in binding affinity can be measured with considerable precision which is a prerequisite for analyzing the functional effect and thermodynamic implications of limited structural changes in interacting molecules. On-rate (ka) and off-rate (kd) kinetic constants of the interaction between virus and antibody can be readily measured and the equilibrium affinity constant K can be calculated from the ratio ka/kd = K.