Consider the following process of folding/unfolding of a tripeptide segment in a large protein. The free energy change $(Δ G)$ will depend on the interaction of the unfolded tripeptide with the solvent (water) and with the rest of the protein in the folded state (see below). Assume that the tripeptide is made up of one non-polar (hydrophobic, shaded) and two polar (hydrophilic; unshaded) residues. Assume the following approximate changes in the interaction free energies:
i) a non-polar residue and the solvent (water), $Δ G = + 8 k J m o l^{- 1}$
ii) a non-polar residue and the rest of the protein, $Δ G = - 4 k J m o l^{- 1}$
iii) a polar residue and the solvent (water), $Δ G = - 16 k J m o l^{- 1}$
iv)a polar residue and the rest of the protein, $Δ G = - 14 k J m o l^{- 1}$

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