Question

The native conformation of a protein is generally the conformation with lowest energy, making protein folding an energetically favorable process. Why then are chaperones and chaperonins required to facilitate this folding

Answer 1

Answer:

The protein folding of a polypeptide is important for the biological function of the protein.  The different types of interaction that plays an important role in protein folding are hydrophobic interaction, covalent and non covalent interaction.

The protein folding is the energetically driven process. But the effective and correct folding requires special molecules like chaperones and chaperonins. These molecule provide proper entropy, helps in the protein assembly and also degrades the misfolded protein.