Chaperonelike

Chaperonelike is an adjective used to describe a molecule, domain, or activity that resembles the functions of a molecular chaperone. Molecular chaperones are proteins that assist other polypeptides in achieving or maintaining properly folded, assembled, and non-aggregated states, often by binding exposed hydrophobic regions, preventing misfolding, or guiding complex assembly. When applied to noncanonical cases, chaperonelike indicates that a protein or RNA exhibits similar protective or catalytic effects on folding or assembly, without necessarily belonging to classical chaperone families or relying on the same ATP-driven cycles.

In practice, chaperonelike activity can be observed in proteins that act as holdases, stabilizing unfolded or partially folded substrates, or in domains within multidomain proteins that transiently assist folding. It is also used for RNA chaperones or RNA chaperone–like activities that facilitate RNA folding without enzymes. The term does not imply an identical mechanism; chaperonelike factors may operate via distinct, ATP-dependent or ATP-independent pathways, and may lack canonical chaperone cofactors.

Usage note: The label is descriptive and comparative, not a formal taxonomy. It signals functional similarity to chaperones and is common in reviews discussing proteostasis, cellular stress responses, or engineered systems designed to mimic chaperone behavior.

See also: molecular chaperone, proteostasis, protein folding, RNA chaperone.