The interaction between membrane proteins and their (protein) ligands is conventionally investigated by nonequilibrium methods such as co-sedimentation or pull-down assays. Surface Plasmon Resonance can be used to monitor such binding events in real-time using isolated membranes immobilized to a surface providing insights in the kinetics of binding under equilibrium conditions. This application provides a fast, automated way to detect interacting species and to determine the kinetics and affinity (K d) of the interaction. © 2013 Springer Science+Business Media, LLC.
CITATION STYLE
Wu, Z. C., De Keyzer, J., Kusters, I., & Driessen, A. J. M. (2013). Analysis of the interaction between membrane proteins and soluble binding partners by surface plasmon resonance. Methods in Molecular Biology, 1033, 157–172. https://doi.org/10.1007/978-1-62703-487-6_11
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