Group I chaperonins are found in eubacteria and the organelles of eubacterial origin, mitochondria and chloroplasts. These chaperonins are named growth E locus, large gene, bacterial group I chaperonin (GroEL), heat shock protein of 60 kDa (Hsp60), and chaperonin of 60 kDa (Cpn60), respectively.

Where are chaperones found?

Chaperonins are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria. Other types of chaperones are involved in transport across membranes, for example membranes of the mitochondria and endoplasmic reticulum (ER) in eukaryotes.

What are chaperonins and what is their role in protein structure?

Chaperonins are protein molecules that assist in the proper folding of other proteins. Their role in protein structure is that they keep the new polypeptide segregated from bad influences in the cytoplasmic environment while it folds spontaneously.