The bacterial chaperonin GroEL significantly assists in the folding of newly synthesized proteins by employing its cofactor GroES to create an enclosed folding chamber.
GroEL's structure consists of two heptameric rings allowing sequential protein folding, utilizing ATP hydrolysis to facilitate the dynamic interaction between substrate proteins and chaperonin.
Studies indicate that GroES binding can shift GroEL's operational mode from asymmetrical to symmetrical, which impacts the mechanism of protein folding assistance provided by GroEL.
GroEL captures unfolded substrate proteins through hydrophobic interactions and assists their proper folding within a chamber, highlighting its crucial role in protein homeostasis in cells.
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