Surface plasmon resonance (SPR) is a robust method to detect and quantify macromolecular interactions; however, to measure binding interactions, one component must be immobilized on a sensor surface. This is typically achieved using covalent immobilization via free amines or thiols, or noncovalent immobilization using high-affinity interactions such as biotin/streptavidin or antibody/antigen. In this chapter we describe a robust method to covalently immobilize His(6) fusion proteins on the sensor surface for SPR analysis.
CITATION STYLE
Kimple, A. J., Muller, R. E., Siderovski, D. P., & Willard, F. S. (2010). A capture coupling method for the covalent immobilization of hexahistidine tagged proteins for surface plasmon resonance. Methods in Molecular Biology (Clifton, N.J.), 627, 91–100. https://doi.org/10.1007/978-1-60761-670-2_5
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