Abstract
Ubiquitin family modifiers (UbFs) are protein–protein interaction modules acting within a variety of cellular processes. In combination with other techniques, surface plasmon resonance (SPR)-based technology has been used to characterize the interactions of UbFs with their binding partners. SPR binding assays allow the real-time detection of binding events with unlabeled analytes, yet are often hindered by the requirement for careful sample preparation and optimized assay conditions. This chapter aims to share our experience in SPR analysis of UbFs and provide helpful hints in sample preparation, experimental design, evaluation, and data interpretation.
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Acknowledgments
This work was supported by a DFG grant (RA1643/2-1) and a grant from the excellence initiative of the University of Konstanz to S.R.
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Stingele, J., Roder, U.W., Raasi, S. (2012). Surface Plasmon Resonance to Measure Interactions of UbFs with Their Binding Partners. In: Dohmen, R., Scheffner, M. (eds) Ubiquitin Family Modifiers and the Proteasome. Methods in Molecular Biology, vol 832. Humana Press. https://doi.org/10.1007/978-1-61779-474-2_19
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DOI: https://doi.org/10.1007/978-1-61779-474-2_19
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