The building blocks of living cells, proteins are enormous collections of nitrogenous organic molecules that are polymers of the amino acids that animals must consume to grow and repair their tissues. ATP-dependent proteins known as chaperones serve as foldases (protein folding assistants), holdases (bind folding intermediates), and disaggregates (convert aberrant protein to monomers). Chaperones include, but are not limited to, DnaJ, DnaK, GrpE, and Hsp33. The majority of chaperones have a cleft containing the nucleotide-binding site that divides the ATPase domain into two subdomains. The features of the C-terminal domain depend on the kind of bound nucleotide. In the presence of ATP, peptides bind and dissociate quickly and with low affinity. In contrast, the affinity increases significantly while the rate of peptide binding reduces when neither ADP nor nucleotide are connected to the N-terminal domain. Hsp90 is a homodimer with a 60 n dissociation constant. In reaction to high temperature or other types of cellular stress that prevent protein folding, several chaperones turn on their activity. Neurodegenerative, Parkinson's, and polyQ diseases, among others, can all be treated with chaperones. This is possible when a protein prevents the accumulation of protein species with improper folding. The suppression of dangerous protein oligomers by clustering, illness response related to protein aggregation, and cancer maintenance are a few new functions for chaperones that are still being discovered.