Temperature jump is a powerful technique for the characterization of fast kinetics and can be readily employed to understand both binding and folding reactions. Here we summarize briefly a temperature-jump prototypical experiment between an intrinsically disordered protein and its physiological partner. The model used is the NTAIL domain from Measles virus Nucleoprotein and its natural ligand, the globular PXD domain from Measles virus Phosphoprotein. We recapitulate how to set up the experiment and how to analyze data in order to extract the kinetic parameters of the reaction.
Keywords: Binding kinetics; Folding and binding; IDP; Intrinsically disordered proteins; Mechanism.