Chemistry (12) Laboratory experiments are being developed for upper-level Physical Chemistry and Biochemistry Laboratory courses that utilize isothermal titration calorimetry (ITC). The exercises include: "Binding Constants of EDTA with Ca(II) and Mg(II) Ions"; "Michaelis-Menten Enzyme Kinetic Study of the Hydrolysis of Benzoylarginine Ether Ester (BAEE) by Trypsin"; "Binding of the N-Acetylglucosamine Trisaccharide ((NAG)3)Ligand to Lysozyme"; and "Investigation of the Interaction of Calmodulin with Ca2+/Calmodulin Kinase II". The binding affinity, reaction enthalpy, and stoichiometric ratio for the two reagents are being obtained directly from the ITC experiments. Additionally, by combining these reaction parameters, it is also possible to determine the reaction entropy and the change in Gibb's free energy for the reaction studied. Program assessment will include the impact of these innovative educational materials on student learning.
Isothermal titration calorimetry is a relatively new technique that is used to determine thermodynamic parameters for small scale reactions. The interdisciplinary nature of isothermal calorimetry makes it a powerful tool to demonstrate the link between discovery and societal benefits such as drug development. Modern, ultrasensitive ITC has found many applications in Biochemistry and Pharmaceutical research: protein-protein, protein-drug, protein-DNA, protein-ligand and metal-ligand interactions are examples of intermolecular interactions that can be studied. Educational materials resulting from these efforts are being nationally disseminated at chemistry education conferences and via manuscripts submitted to professional journals.
