in vivo, and moreover are underrepresented on ribosomes translating inner membrane proteins. TF not only directly works to properly fold the protein but also recruits other chaperones to the ribosome, such as Hsp70. Hsp70 surrounds an unfolded peptide chain, thereby preventing aggregation and promoting folding.

Chaperonins are a special class of chaperones that promote native state folding by cyclically encapsulating the peptide chain. Chaperonins are divided into two groups. Group 1 chaperonins are