Chaperone proteins are a class of proteins that assist in the proper folding and unfolding of other proteins, while also preventing the aggregation of misfolded proteins. They play a crucial role in maintaining protein homeostasis within cells by ensuring that newly synthesized proteins assume their functional three-dimensional structure and by helping to refold denatured proteins that result from cellular stress. Chaperone proteins also act as quality control mechanisms by targeting misfolded proteins for degradation or assisting in their refolding. Dysfunction of chaperone proteins has been linked to various neurodegenerative diseases, cancer, and other pathologies. Overall, chaperone proteins are essential for maintaining protein stability and function in the cell, making them a key area of research in understanding cellular processes and developing potential therapeutic strategies for various diseases.