Abstract

Molecular chaperones are essential proteins that facilitate the correct folding, assembly, and maintenance of other proteins within the cell. Their primary role is to prevent misfolding and aggregation of nascent and stress-denatured proteins, thereby ensuring cellular proteostasis and functionality. This abstract reviews the fundamental mechanisms by which molecular chaperones operate, including their involvement in protein folding pathways, quality control processes, and stress responses. The major classes of molecular chaperones, such as heat shock proteins (HSPs), chaperonins, and co-chaperones, are discussed in terms of their specific functions and interactions. Additionally, the abstract highlights the implications of chaperone dysfunction in various diseases, including neurodegenerative disorders and cancer, underscoring their potential as therapeutic targets. The ongoing research into molecular chaperones continues to reveal their intricate roles in cellular health and disease, paving the way for novel strategies in disease management and treatment.