Question

Question 20. Chaperones assist proteins to fold by

A. Catalyzing the folding of alpha helices and beta sheets

B. Catalyzing the formation of peptide bond

C. Binding hydrophobic amino acids in the polypeptide chain and preventing non specific hydrophobic interactions

D. Binding charged amino acids in the polypeptide chain and shielding them from water

Answer 1

Ans .(20) option (C) Binding hydrophobic amino acids in the polypeptide chain and preventing non specific hydrophobic interactions.

Folding of polypeptides in the cell typically requires the assistance of a set of proteins termed molecular chaperones. Chaperones are an essential group of proteins necessary for cell viability under both normal and stress conditions.

A typical feature of chaperones is the stoichiometric and transient binding of non-native polypeptides mostly at exposed hydrophobic patches.

Chaperones binding stabilizes productive folding intermediates, hinders non-native proteins from building incorrect intramolecular and intermolecular interactions and in this way reduces protein misfolding and aggregation.