Lecture
This lecture by the instructor delves into the intricate process of protein folding, exploring how proteins achieve their functional native state through energy landscapes. The discussion covers the role of chaperones in assisting protein folding, the impact of entropy on folding reliability, and the stabilization of native states. The lecture also examines the mechanisms of molecular chaperones like GroEL and Hsp70, highlighting their ATP-driven cycles and their ability to maintain proteins in a non-equilibrium state. Through experimental results and theoretical models, the lecture sheds light on the non-equilibrium nature of protein folding, challenging traditional views based on thermodynamic equilibrium.