Hydrophobic Interactions Hydrophobic interactions minimizes interactions of non-polar residues with solvent. Thus nonpolar regions of biological macromolcules are often buried in the molecules interior to exclude them from the aqueous milieu. However non-polar residues can also be found on the surface of a protein.They may participate protein-protein interactions. This type of interaction is entropy driven. Hydrophobic Interactions Hydrophobic interactions minimizes interactions of non-polar residues with solvent. Thus nonpolar regions of biological macromolcules are often buried in the molecules interior to exclude them from the aqueous milieu. However non-polar residues can also be found on the surface of a protein. They may participate protein-protein interactions. This type of interaction is entropy driven