Hello
I've collected ITC data and I'm not sure if this data looks correct. This was an experiment meant to understand the properties of an enzyme thought to be active as a dimer. The sample cell was filled with buffer and the syringe with the enzyme. I calculate a Kd of 1.73 µM. How would I go about calculating the other thermodynamic properties like enthalpy of protein unfolding (ΔH), entropy changes (ΔS), and the Gibbs free energy change (ΔG) associated with protein stability. I'm including an image of the ITC. I would appreciate any feedback on whether this is good data or I should troubleshot some more. Any advice or thoughts on the data would be appreciated.
The Gibbs energy can be calculated from the dissociation constant, but for the dissociation enthalpy you must rely on the software data analysis, which should provide all the interaction parameters (at least, affinity and enthalpy).
Thanks for the response Adrian. Followup question, is the data that was presented publishable, once I provide the Gibbs free energy and the other parameters. To be clear, there is no interaction being measured in this experiment between a ligand and an enzyme. This is just the enzyme in the syringe into a buffer only filled cell.
With that experiment you are determining the parameters for dissociation (or self-association) of the dimeric protein. This information could be interesting from the point of view of the enzyme characterization and understanding its behavior in its natural environment or for industrial applications.
But, eventually, you should judge whether this information is interesting.
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