Final answer:
Hydrophobic interactions in water-soluble proteins primarily occur in the interior of the protein, where non-polar amino acids interact with each other through hydrophobic interactions.
Step-by-step explanation:
Hydrophobic interactions are most likely to occur in the interior of a water-soluble protein.
Polar and charged amino acids will be found on the surface of the protein, while non-polar amino acids will be found in the interior where they can interact with each other through hydrophobic interactions.
These hydrophobic interactions occur when hydrophobic groups come close to each other, expelling water away from those regions.