title: Surface plasmon resonance to measure interactions of UbFs with their binding partners.
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.
authors.affiliation: Department of Molecular Cell Biology, Max-Planck Institute of Biochemistry, Martinsried, Germany.
authors.forename: Julian
authors.initials: J
authors.lastname: Stingele
authors.forename: Uwe W
authors.initials: UW
authors.lastname: Roder
authors.forename: Shahri
authors.initials: S
authors.lastname: Raasi
mesh_terms: D015374:Biosensing Techniques / Q000379:methods; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs / Q000502:physiology*; D020349:Surface Plasmon Resonance / Q000379:methods*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism
chemical_list: D025801:Ubiquitin