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This general term pertains to a large group of multifunctional proteins that interact with other proteins and assist in proper folding, maturation, unfolding, intracellular trafficking, and also degradation of these client proteins. Many chaperones are heat shock proteins. Some chaperones are specific for certain types of proteins (e. g., for collagens or histones), but most chaperones bind clients promiscuously and even a single chaperone can use many different mechanisms to aid in these processes by preventing non-specific interactions with other surrounding proteins. The term cochaperone refers to proteins that regulate the activity of chaperone proteins and may even switch chaperone complexes from protein folding to protein degradation (for overview see: Melnyk et al, 2015; Ellgaard et al, 2016; Bar-Lavan et al, 2016; Koldewey et al, 2070).

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