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Chaperonin | Wikipedia
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein … See more
The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. Each ring is composed of either … See more
Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic hydrolysis of ATP as well as binding of substrate proteins and … See more
As mentioned, all cells contain chaperonins.
• In bacteria, the archetype is the well-characterized chaperonin GroEL from E. coli.
• In archaea, the chaperonin is called the thermosome See moreGroup I
Group I chaperonins (Cpn60) are found in bacteria as well as organelles of endosymbiotic origin: chloroplasts and mitochondria.
The GroEL/GroES complex in E. coli is a Group I chaperonin … See moreHuman GroEL is the immunodominant antigen of patients with Legionnaire's disease, and is thought to play a role in the protection of the … See more
Wikipedia text under CC-BY-SA license Chaperonin Definition & Meaning | Merriam-Webster Medical
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WEBAug 20, 2019 · Chaperones are a type of molecular chaperones responsible for the folding and assembly of proteins into their native structures. Moreover, they are responsible for the remodeling of proteins with …
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