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 …

To elucidate the exact role of the helical protrusion of a group II chaperonin in its molecular
chaperone function, three deletion mutants of the chaperonin from a hyperthermophilic …

The gene encoding the beta subunit of a molecular chaperonin from the hyperthermophilic
archaeon Pyrococcus sp. strain KOD1 (cpkB) was cloned, sequenced, and expressed in …

Chaperonins are among the most abundant proteins in thermophilic and hyperthermophilic
microorganisms. A fast and efficient protocol has been designed to purify chaperonins from …

The Hsp60/Chaperonin family of molecular chaperones assists in protein folding and can be
classified into two large groups: The seven-fold symmetric groupI chaperonins from bacteria …

Type I chaperonins play an essential role in the folding of newly translated and stress-
denatured proteins in eubacteria, mitochondria and chloroplasts. Since their discovery, the …

Group II chaperonins, found in Archaea and in the eukaryotic cytosol, act independently of a
cofactor corresponding to GroES of group I chaperonins. Instead, the helical protrusion at …

In all three kingdoms of life chaperonins assist the folding of a range of newly synthesized
proteins. As shown recently, Archaea of the genus Methanosarcina contain both group I …

It is apparent that a major sub-set of heat shock proteins assist other polypeptides to
maintain, or assume, a conformation required for their correct assembly into biologically …

Chaperonins (Hsp60 chaperones) comprise a class of oligomeric, high-molecular-weight
chaperones that have the unique ability to fold some proteins that cannot be folded by …