Final answer:
The tertiary structure of proteins is stabilized by hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide linkages, all of which contribute to the protein's three-dimensional shape and functionality.
Step-by-step explanation:
The tertiary structure involves long-range interaction between amino acids through hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide linkages . These interactions are essential for the overall three-dimensional formation of the protein, impacting its stability and function. For instance, hydrophobic interactions occur when nonpolar amino acids are repelled by the surrounding water, causing them to aggregate in the protein's interior, while polar amino acids tend to be positioned on the protein's surface. Ionic bonds are formed between amino acids with charged R groups that are attracted to each other, and hydrogen bonds can form between hydrogen atoms and nearby oxygen, nitrogen, or sulfur atoms. Disulfide bridges, the covalent bonds between the sulfur atoms of two cysteine amino acids, provide additional stabilization of the protein structure in the presence of oxygen.