Human thymidylate synthase ITC data

This dataset includes isothermal titration calorimetry measurements of
human thymidylate synthase (hTS) binding its product deoxythymidine
monophosphate (TMP) and an N-terminal trunction of hTS binding its
substrate deoxyuridine monophosphate (dUMP). These measurements include
heats produced at various enzyme and ligand concentrations. Analysis of
these data provide binding free energies, enthalpies, and entropies for
these binding events. We find that in contrast to hTS binding its
substrate dUMP, which we have previously shown to have positive
cooperativity, hTS binding TMP and the N-terminally truncated hTS binding
dUMP are non-cooperative. Details of the data collection and analysis can
be found in the associated publication.