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
1. A GroEL ring binds an unfolded polypeptide and 7 ATP
2. GroES binds to GroEL, causing a conformational shift and displacing the polypeptide into the cavity
3. ATP is hydrolyzed and the polypeptide, isolated from interfering contact, folds
4. The GroES "cap" dissociates from the GroEl ring
5. ADP and the folded polypeptide and released as ATP and GroEs bind to the other GroEL ring