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This lecture covers the principles of determining the affinity between proteins and ligands, focusing on concepts such as binding isotherms, drug development criteria, and the energetics of binding reactions. It discusses methods like Isothermal Titration Calorimetry (ITC), Surface Plasmon Resonance (SPR), and NMR for measuring binding affinity and kinetics. The instructor explains the relationship between thermodynamics and kinetics in protein-ligand interactions, highlighting the importance of understanding both aspects for drug development.