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Surface plasmon resonance (SPR) is an optical phenomenon in which light is being absorbed by electrons on a thin metal surface, thereby resonating the electrons and causing a reduction of light intensity and reflection at a specific angle (i.e., SPR angle). The technique is commonly used to study molecular interactions, especially protein-protein interactions. Important interaction parameters, such as binding affinities and kinetics can be measured. The main advantages of SPR-based analysis are that molecular interactions can be studied in real time, and in a label-free environment, with relatively small quantities of binding partners required compared to such other techniques as isothermal titration calorimetry (ITC). Besides, SPR-based analysis is one of the most effective approaches for detecting highly dynamic molecular interactions, for example, interaction of secreted proteins in bacterial cells.

The Sierra SPR-32 Pro Analyser available at the ULS is a high-sensitivity, high-throughput system for SPR-based analyses. This system is equipped with a so-called SPR+ detector with improved signal-to-noise ratio and higher sensitivity for small response changes.

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