This lecture focuses on the life cycle of proteins, emphasizing their folding, maturation, and degradation processes. It begins with a review of protein translation and the emergence of their three-dimensional structures. The instructor explains the different levels of protein structure, including primary, secondary, tertiary, and quaternary structures, and discusses the interactions that stabilize these formations, such as covalent bonds, ionic bonds, and hydrophobic interactions. The role of chaperones in assisting proper protein folding is highlighted, detailing how they prevent misfolding and aggregation. The lecture also addresses the consequences of incorrect folding, including the formation of toxic aggregates and their association with various neurodegenerative diseases, such as Alzheimer's, Parkinson's, and prion diseases. The importance of maintaining protein integrity within the cell is underscored, as misfolded proteins can lead to severe cellular dysfunction. Overall, the lecture provides a comprehensive overview of protein dynamics and their critical roles in cellular health.