Quantitative Characterization of Biomolecular Interactions - SPR
Surface Plasmon Resonance
SPR is a chip-based technology to measure biomolecular interactions in a label free environment in real-time. As one of the interactants is immobilized to the sensor surface, the others are free in solution and passed over the surface. Formation and dissociation are measured in arbitrary units and displayed in a graph called the sensorgram. From this sensorgram, various kinetic parameters can be calculated (ex.on-rates, off-rates and affinities)
Biomolecular interaction analysis is not limited to proteins. DNA-DNA, DNA-protein, lipid- protein and hybrid systems of biomolecules and non-biological surfaces can be investigated.
Biomolecular interaction analysis can be used to:
- Identify the binding of two or more interactants to each other
- Determine the strength of binding of the interactions
- Measure the kinetic rates of reaction (actual formation and dissociation rates).
- Quantify the concentration of protein in a complex mixture after binding
A Biacore 3000 SPR instrument is now available for use. The equipment is located in room C2705. Most analyses require a day to set up and run. Hourly or weekly rates are available. Please contact Wade Edris firstname.lastname@example.org to reserve time or for fee information.