Harkness V, Robert WSlavkovic, SladjanaJohnson, Philip E.Mittermaier, Anthony K.2023-05-102023-05-102016-10-23Chem. Commun. 52 (2016): 13471--13474https://doi.org/10.1039/c6cc05576ahttp://hdl.handle.net/10315/41140Differential scanning calorimetry (DSC) is a powerful technique for measuring tight biomolecular interactions. However, many pharma- ceutically relevant ligands are chemically unstable at the high temperatures used in DSC analyses. Thus, measuring binding inter- actions is challenging because the concentrations of ligands and thermally-converted products are constantly changing within the calorimeter cell. Using experimental data for two DNA aptamers that bind to the thermolabile ligand cocaine, we present a new global fitting analysis that yields the complete set of folding and binding parameters for the initial and final forms of the ligand from a pair of DSC experiments, while accounting for the thermal conversion. Furthermore, we show that the rate constant for thermolabile ligand conversion may be obtained with only one additional DSC dataset.enAttribution-NonCommercial-NoDerivatives 4.0 InternationalArticle