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 …

Chaperonins are required for correct folding of many proteins. They exist in two phylogenetic
groups: group I, found in bacteria and eukaryotic organelles, and group II, found in archaea …

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” …

Chaperonins are a class of molecular chaperones that form large multimeric assemblies for
encapsulation of substrate proteins. Surprisingly, 30% of newly sequenced bacterial …

Chaperonins are a subgroup of the molecular chaperone family of proteins. In an ATP-
dependant manner, chaperonins promote the folding of newly synthesized proteins to the …

Chaperonin action is controlled by cycles of nucleotide binding and hydrolysis. Here, we
examine the effects of nucleotide binding on an archaeal group 2 chaperonin. In contrast to …

Abstract In 1973, Christian Anfinsen and coworkers noted that accelerated protein folding in
intact cells and cell extracts suggested that a “disulfide interchange enzyme” might be …

Chaperonins are a class of molecular chaperones that assemble into a large double ring
architecture with each ring constituting seven to nine subunits and enclosing a cavity for …

Chaperonins are a subclass of molecular chaperones that assist both the folding of newly
synthesized proteins and the maintenance of proteins in a folded state during periods of …

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