Facilities: Biacore SPR
Surface plasmon resonance (SPR) technology allows for quantitative, real-time biomolecular interaction analysis. Using purified preparations or complex mixtures, binding interactions between proteins, lipids, carbohydrates, nucleic acids, small molecules, and cells/viruses can be examined in their native state with low sample consumption. In a typical experiment, the ligand (‘bait’) is immobilized to a gold-plated sensor chip and repeated injections of analyte (binding partner ‘target’) are then flowed overtop. A variety of sensor chip surfaces (eg. dextran, streptavidin, antibodies) and immobilization chemistries (eg. amine, biotin, thiol) are available to tailor your research needs. Analyte-ligand association and dissociation events are monitored by changes in molecular mass accumulation at the solid-liquid interface on the sensor chip surface. The acquired data can answer questions regarding specificity, stoichiometry, concentration, kinetics (ka, kd), and overall affinity (KD=kd/ka). In ligand fishing experiments, unknown binding partners can also be recovered for subsequent identification by mass spectrometry (SPR-MS).
Our facility includes one Biacore 3000 SPR instrument located in A112 Engineering Quadrangle. All users are required to be trained before they are given access to the instrument. Users must reserve a time slot on our online calendar system.
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