Chaperonins are ubiquitous and essential protein folding machines. They have a striking
structure, with two rings of seven, eight, or nine protomers forming a “double doughnut” …

The chaperonin proteins form a ubiquitous family of molecular chaperones and are
absolutely required for correct folding or assembly of a subset of proteins in the cell. They …

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 …

Two distantly related classes of cylindrical chaperonin complexes assist in the folding of
newly synthesized and stress-denatured proteins in an ATP-dependent manner. Group I …

Thermophilic organisms tolerate or adapt to high temperatures by making their proteins
thermostable or thermophilic. Even though, thermophilic bacteria have their own optimal …

The Hsp60 or chaperonin class of molecular chaperones is divided into two phylogenetic
groups: group I, found in bacteria, mitochondria and chloroplasts, and group II, found in …

We have cloned and sequenced the genes encoding two chaperonin subunits (Cpn-α and
Cpn-β), from Archaeoglobus fulgidus, a sulfate-reducing hyperthermophilic archaeon. The …

It is now well understood that, although proteins fold spontaneously (in a thermodynamic
sense), many nevertheless require the assistance of helpers called molecular chaperones to …

Thermococcus kodakaraensis KOD1 produces two kinds of chaperonin subunits, CpkA and
CpkB. To monitor the expression levels of CpkA and CpkB, anti-CpkA and anti-CpkB …

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 …