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This lecture explores the non-equilibrium dynamics of protein folding, discussing the challenges proteins face in maintaining their native state and the role of molecular chaperones in preventing misfolding and aggregation. The instructor delves into the mechanisms of chaperones like GroEL and Hsp70, highlighting their ATP-driven cycles and their impact on protein stability. Through experiments and models, the lecture showcases how chaperones maintain proteins in a non-equilibrium steady state, challenging traditional views of protein thermodynamics. The implications of chaperone-assisted folding on protein biophysics and evolution are also discussed, shedding light on the potential for faster evolution and adaptation in changing environments.