Where are hydrophobic interactions most likely to occur?

Hydrophobic effect is the tendency of non polar molecules (hydrophobic) in a solvent that is polar to interact with each other resulting to a hydrophobic interaction. These non polar molecules are called hydrophobes and are made of long chains of carbon that are water hating (do not interact with water). In this case, the hydrophobic interactions are most likely to occur on the core of a water soluble protein.

Hydrophobic interactions most likely to occur in the core of a water-soluble protein in which side chains are buried from water, which stabilizes the folded state. This charged side chains are located on the solvent-exposed surface where they interact with immediate water molecules. In addition, the creation of hydrogen bonds within the protein also stabilizes protein structure.