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Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1 MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner.
2 Μαΐ 2018 · Based on the various structural and functional studies carried out by our group since the last decade on the chaperonin GroEL/ES system, we have better understood the importance of this system...
1 Αυγ 2011 · The nested allosteric cooperativity model combines both the MWC and KNF models to explain the positive intra-ring and negative inter-ring cooperativity in chaperonins. This concept is particularly useful in the case of large oligomeric proteins with a hierarchical structure.
This chapter concerns structural aspects of the GroEL/GroES chaperonin– mediated protein folding reaction. It first reviews the overall cellular actions of bacterial and organellar chaperonins (the so-called type I chaperonins), as well as the discovery and early EM imaging of these ring assemblies.
Chaperonins are a class of molecular chaperone composed of oligomeric double-ring protein assemblies that provide essential kinetic assistance to protein folding by binding non-native proteins and allowing them to fold in the central cavities of their rings.
Chaperonins are classified into two distantly related structural groups: Group I is found in bacteria (GroEL) and eukaryotic organelles (Hsp60), and Group II is expressed in Archaea (thermosome) and in the eukaryotic cytosol (chaperonin containing TCP1 (CCT), or TCP1 ring complex (TRiC)) (Kim, Hipp, Bracher, Hayer-Hartl, & Hartl, 2013).
11 Απρ 2018 · Chaperonins are a subclass of molecular chaperones that assist cellular proteins to fold and assemble into their native shape. Much work has been done on Type I chaperonins, which has elucidated their elegant mechanism.
