Chaperonins are multisubunit protein-folding assemblies. They are composed of two distinct
structural classes, which also have a characteristic phylogenetic distribution. Group I …

Chaperonins are oligomeric protein-folding complexes which are divided into two distantly
related structural classes. Group I chaperonins (called GroEL/cpn60/hsp60) are found in …

Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …

Chaperonins are key components of the cell machinery and are involved in the productive
folding of proteins. Most chaperonins share a common general morphology based in a …

Chaperonins (CPN) are ubiquitous oligomeric protein machines that mediate the ATP-
dependent folding of polypeptide chains. These chaperones have not only been assigned …

Publisher Summary This chapter discusses the structure and function of chaperonins in
archaebacteria. It is possible that chaperonin-containing TCP-1 (CCT) evolved solely to …

Publisher Summary Chaperonin homologs are found in all extant species, including
eubacteria, archaebacteria, and eukaryotes. In bacteria and eukaryotic cell organelles, such …

Chaperonins are essential biological complexes assisting protein folding in all kingdoms of
life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non …

Chaperonins are multi-subunit double-ring complexes that mediate the folding of nascent or
denatured proteins. Gene duplication has been a potent force in the evolution of …

The cytosolic chaperonin CCT is a 1‐MDa protein‐folding machine essential for eukaryotic
life. The CCT interactome shows involvement in folding and assembly of a small range of …