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Put the following steps of GroEL-GroES chaperonin function in order, starting with an unfolded polypeptide and...

Put the following steps of GroEL-GroES chaperonin function in order, starting with an unfolded polypeptide and ending with a polypeptide in its native conformation.

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Answer #1

A GroEL ring binds an unfolded polypeptide on its hydrophobic surfaces.

ATP and GroES bind to the GroEL ring, causing a conformational change and displacing the unfolded polypeptide into the cavity.

Inside the cavity, the polypeptide can fold without interference from other molecules or ions.

ATP hydrolysis causes conformational changes that result in the dissociation of the GroES cap from the GroEL ring.

The folded polypeptide (and seven ADP) are released from the GroEL ring as ATP and GroES bind to the other GroEL ring.

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