An understanding of the thermodynamics of protein�ligand binding is important for insight into molecular interactions. In this study, the binding of the mouse major urinary protein-I (MUP-I) to ligands is being explored by isothermal titration calorimetry (ITC) and X-ray crystallography. This protein is characterized by enthalpy-driven binding with nonpolar ligands in a hydrophobic pocket, a phenomenon that has been called a �nonclassical� hydrophobic effect. The synthesis of a pyridazine analogue of the known ligand 2-methoxy-3-isobutylpyrazine is being optimized, and studies using ITC have revealed the thermodynamic effects of the structural changes. Crystal structures are currently being solved of the protein-ligand complexes of MUP-I with 3-isobutyl-4-methoxypyridazine and other nitrogen heterocycles, and these results will be reported.

Thermodynamic effects of structural changes in protein-ligand interactions

247th National Meeting (2014)

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