Question

From a thermodynamic point of view, how does a protein fold into its native and functional structure?

Answer 1

Answer ----->

Protein folding is driven entirely by entropy.water plays a large role in protein folding. In unfolded protein water is ordered and polypeptide chain is disordered but during folding the release of disordered water upon aggregation causes an increase in entropy .

In fact, hydrophobic domains of a protein constrain the possible configurations of surrounding water and so their burial upon folding increases the water’s entropy. Moreover, it turns out that the hydrogen bonding of polar residues and the backbone is satisfied both in an unfolded state (by water) and in a folded state (by each other). Therefore enthalpy is “zero sum,” and protein folding is driven almost entirely by entropy.