Integrated Native ESI-IM-MS Studies for Thermodynamic Comparison of H2O vs. D2O on Protein Complex-ligand Binding Reactions

Dissecting the thermodynamics for binding ligands to protein complexes one ligand at a time reveals new insights on the influence of H2O and D2O. Here, studies employ variable-temperature ESI and native ion mobility-mass spectrometry approaches for dissecting the binding one ligand at a time. The goals for these studies are to provide more in depth understanding of the role of hydration on structure, stabilities and dynamics protein-ligand binding of protein-ligand complexes. Results from studies of both chaperones-nucleotide binding (GroEL-ATP/ADP) and membrane protein complex lipid binding will be presented. These studies also provide detailed thermodynamics determinations (G, H and -TS), including enthalpy-entropy compensation (EEC).