Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …

Chaperonins are large ring assemblies that assist protein folding to the native state by
binding nonnative proteins in their central cavities and then, upon binding ATP, release the …

Metagenomics has provided access to genomes of as yet uncultivated microorganisms in
natural environments, yet there are gaps in our knowledge—particularly for Archaea—that …

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 …

Thermoacidophilic archaea belonging to the order Sulfolobales thrive in extreme biotopes,
such as sulfuric hot springs and ore deposits. These microorganisms have been model …

This review is focused on the mechanisms by which ATP binding and hydrolysis drive
chaperone machines assisting protein folding and unfolding. A survey of the key, general …

The chaperonins are a family of molecular chaperones present in all three kingdoms of life.
They are classified into Group I and Group II. Group I consists of the bacterial variants …

Chaperonins are molecular machines that facilitate protein folding by undergoing energy
(ATP)-dependent movements that are coordinated in time and space by complex allosteric …

Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-
dependent movements that are coordinated in time and space owing to complex allosteric …