Final answer:
Water has a strong impact on the tertiary structure of proteins, which is influenced by the hydrophobic and hydrophilic properties of the amino acid side chains; thus, Water has a strong effect on tertiary structure.
Step-by-step explanation:
The presence of both polar and nonpolar side chains in a protein predominantly affects its tertiary structure. Water influences this level of protein structure significantly due to the distinct interactions that occur between the water molecules and the different side chains. Water has a strong effect on tertiary structure.
In proteins, nonpolar, hydrophobic side chains tend to cluster away from water, whereas polar, hydrophilic side chains interact with water and are typically found on the protein's surface. The three-dimensional folding, vital for the protein's functionality, is largely driven by the hydrophobic and hydrophilic interactions. Therefore, the tertiary structure will be significantly affected by water, which promotes the folding process and helps stabilize the folded protein through hydrophobic interactions, hydrogen bonds, and ionic interactions. In contrast, covalent disulfide bonds, formed by the oxidation of cysteine residues, provide further stability to the protein's tertiary structure, illustrating the complexity of protein conformation.