Disease states such as AZ and Huntington's are thought to be related to amyloid plaques resulting from proteins that are misfolded. Chaperonins assist to make sure proteins fold correctly as well as unzip misfolded proteins to give them a second chance at folding properly. So my question is this, what makes sure that the chaperonins themselves fold correctly? Are there chaperonins of chaperonins? If so, what would make sure chaperonins of chaperonins fold correctly (of course you could keep continuing this logic)? Rather than studying the misfolding and polymerization of misfolded proteins that lead to amyloids, has anyone done research on whether or not the chaperonins that are supposed to be regulating the misguided protein folding are themselves misfolded?