Ricerc@Sapienza

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.

The already known di(2-pyridyl)dihydropyrazine (dhdpp) was prepared and isolated also in the form of a bis-hydrated species, i.e., dhdpp·2H2O. As established by X-ray work, a small amount of single crystals of di(2-pyridyl)-pyrazine (dpp) was also obtained from the mother liquors, this testifying the possibility of a dehydrogenation process dhdpp → dpp in the absence of a catalyst.