Surface Plasmon Resonance offers several advantages that make it a widely used technique in various scientific disciplines. Firstly, it provides label-free and real-time measurements, eliminating the need for fluorescent or radioactive labeling of biomolecules. This allows for more accurate and physiologically relevant data.
Secondly, Surface Plasmon Resonance can determine kinetic parameters, such as association and dissociation rates, and equilibrium constants, providing valuable insights into binding events. Additionally, SPR can be used to study a wide range of biomolecular interactions, including protein-protein interactions, DNA-protein interactions, and small molecule-protein interactions.
However, like any technique, SPR also has its limitations. It requires careful surface preparation to immobilize the ligands, and the technique is generally limited to studying interactions that occur near the metal surface. Furthermore, SPR does not provide information about the structural details of the binding complex.
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