There are a great number of different co-chaperones however based on their domain structure most of them fall into two groups: J-domain proteins and tetratricopeptide repeats (TPR).
Co-chaperones catalyze the hydrolysis ATP to ADP on their respective chaperones which then allows them undergo a large conformational change that allows them to either bind to their substrates with higher affinity or aid in the release of the substrate following protein folding, as in the case of co-chaperone p23.
[3] The mechanism of TPR proteins is less studied these domains have been shown to interact with Hsp90 and Hsp70 and may be involved in the creation of an Hsp70-Hsp90 multi-chaperone complex.
An interaction between Hsp90 and its co-chaperone, Aha1, is essential to the proper folding of cystic fibrosis transmembrane conductance regulator (CFTR).
Co-chaperones CSPα (DNAJC5), auxilin (DNAJC6) and RME-8 (DNAJC13) are important for preserving folding and assembly, therefore preventing protein aggregation.