Chaperones are proteins that assist in correct folding of other proteins, a proc

Question

Chaperones are proteins that assist in correct folding of other proteins, a process determined primarily by the primary [____] in the substrate protein. The interaction depends upon the chaperone recognizing [____] in the substrate proteins that are normally buried in the interior. As an example, a misfolded, non-native substrate protein binds to the hydrophobic surfaces within the cavity of [____]; the binding of [____] causes a change of conformation and the cavity surfaces become [____], thereby releasing the substrate to attempt to refold correctly. Rebinding of non-native proteins initiates a new cycle.

(1) shape; hydrophillic domains; GroEL; Hsp70; hydrophobic

(2) amino acid sequence; hydrophillic domains; Hsp70; ATP; hydrophobic

(3) structure; mis-folded amino acids; Hsp60; ATP; hydrophobic

(4) hydrophobic amino acids; mis-folded domains; Hsp70; Hsp60; hydrophillic

(5) amino acid sequence; hydrophobic domains; GroEL; ATP; hydrophilic

Explanation / Answer

(5) amino acid sequence; hydrophobic domains; GroEL; ATP; hydrophilic

GroEL belongs to the family of chaperonins. The substrate proteins which are to be folded identify a hydrophobic patch in the open cavity if the GroEL complex and form a binary complex with it. After that ATP binds and causes a conformational change which facilitates proper folding. Other than these factors their are other factors too which assist in folding.

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