Protein Folding: Free Energy and Interactions

This lecture covers the concept of free energy in protein folding, including the energetic determinants and protein-protein interactions. It explains the role of entropy and enthalpy in spontaneous reactions, equilibrium constants, and examples like ATP hydrolysis. The lecture also delves into acid-base equilibrium, protonation states, and the hydrophobic effect. It discusses the thermodynamic properties of proteins, focusing on calorimetry and unfolding reactions. Furthermore, it explores the importance of binding in cellular processes, the energetic landscape of binding, and binding affinity. The relationship between affinity and specificity in protein-ligand interactions is highlighted, along with the determination of equilibrium constants and processes controlled by binding.