Final answer:
Hydrophobic interactions, like disulfide linkages, are common inside proteins, away from water. Ionic bonds and hydrogen bonds are more prevalent on the hydrophilic protein surface, which interacts with water.
Step-by-step explanation:
Types of bonds are apt to be more common in the non-aqueous:
Hydrophobic interactions and disulfide linkages are more common in the non-aqueous, interior environment of a protein, while hydrogen bonding and ionic interactions are prevalent on its aqueous surface. In the protein’s interior, non-polar amino acids dominate because they are hydrophobic and avoid contact with water. Polar and charged amino acids are typically found on the protein surface, interacting with the aqueous environment.
For example, disulfide linkages between two cysteine amino acid units stabilize the protein's tertiary structure, and are found in proteins such as insulin. On the other hand, ionic bonds and hydrogen bonds help maintain protein structure and are profoundly influenced by the presence of water. Therefore, these polar interactions are more common on the protein surface that is exposed to an aqueous environment.