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Updated: Dec 14, 2025

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions
1Department for Biophysical Chemistry, Center for Molecular Protein Science, LTH, Lund University, Lund, Sweden. kristine.steen_jensen@bpc.lu.se.
Abstract:
Many intrinsically disordered proteins (IDPs) adopt a well-defined structure upon binding to their interaction partners. Kinetic characterization is a requirement for the investigation of the dynamics and mechanisms of these folding-upon-binding reactions. Here a protocol is described for the investigation of binding kinetics of bimolecular binding and folding reactions of IDPs to their ligand partner under pseudo-first-order conditions using stopped-flow mixing and fluorescence detection.
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