In an aqueous (water) environment, polar (hydrophilic) regions of a protein tend to be on the surface where they can interact with water, while non-polar (hydrophobic) regions tend to be buried in the interior of the protein to avoid contact with water. Therefore, when a polypeptide folds in water, the most likely arrangement would be:
B. The polar region is exposed on its surface and the non-polar region is interior.
This arrangement minimizes the free energy of the system by maximizing interactions with water for the polar regions and minimizing exposure to water for the non-polar regions.