In archaea, prefoldins are believed to function in combination with group II chaperonins[2] in de novo protein folding.

Actin is made of two strings of beads wound round each other and is one of the three main parts of the cytoskeleton of eukaryotic cells.

[3] For example, the prefoldin that is used in the formation of actin also transfers α or β tubulin to a cytosolic chaperonin.

Unlike many other molecular chaperones, prefoldin does not use chemical energy, in the form of adenosine triphosphate (ATP), to promote protein folding.

[5] Prefoldin was found by the laboratory of Nicholas J. Cowan from the Department of Biochemistry at the New York University Medical Center.

This solution contained an excess of cytosolic chaperonin (C-CPN), a eukaryotic chaperone protein necessary for actin folding.

[2] The subunits are arranged by hydrophobic interactions with two β barrels at the center and coiled-coil α helices protruding down from them as if it were a jellyfish.