Archaeal Group II chaperonins (Cpns) are strongly conserved, considering that their growth
temperatures range from 23 to 122° C. The C-terminal 15–25 residues are hypervariable …

Chaperonins are a type of molecular chaperone that assist in the folding of proteins. Group II
chaperonins play an important role in the proteostasis in the cytosol of archaea and eukarya …

Chaperonin is a double ring-shaped oligomeric protein complex, which captures a protein in
the folding intermediate state and assists its folding in an ATP-dependent manner. The …

The functional characteristics of group II chaperonins, especially those from archaea, have
not been elucidated extensively. Here, we performed a detailed functional characterization …

The chaperonins (CPNs) are megadalton sized hollow complexes with two cavities that
open and close to encapsulate non-native proteins. CPNs are assigned to two sequence …

Group II chaperonins exist in archaea and the eukaryotic cytosol, and mediate protein
folding in an ATP-dependent manner. We have been studying the reaction mechanism of …

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

Chaperonins are double-ring protein assemblies with a central cavity that provides a
sequestered environment for in vivo protein folding. Their reaction cycle is thought to consist …

The ATP-dependence of folding chamber closure in the 16-subunit homo-oligomeric
chaperonin from archaea Methanococcus maripaludis (Mm-cpn) has been studied by single …

The hyperthermophilic archaeon Pyrococcus furiosus (Pf) grows optimally at 100° C and
encodes single genes for the Group II chaperonin (Cpn), Pf Cpn and α-crystallin homolog …