Final answer:
E, Hydrogen bonds are crucial for stabilizing the tertiary structure of proteins due to their abundance and ability to form between polar amino acid side chains and the protein backbone.
Step-by-step explanation:
The tertiary structure of proteins is stabilized by a variety of forces including especially important hydrogen bonds. Hydrogen bonds can form between highly electronegative atoms like oxygen or nitrogen and a hydrogen atom that is covalently bonded to another electronegative atom. This type of bonding is more numerous than the other forces, such as ionic bonding, disulfide linkages, and dispersion forces when it comes to stabilizing the tertiary structure of proteins. Moreover, hydrogen bonds play significant roles in both intra- and intermolecular interactions within proteins. Many polar amino acid side chains form hydrogen bonds, contributing to the protein's overall stability. These bonds are not necessarily stronger than the other forces, like ionic bonds or covalent disulfide bridges; instead, the abundance and versatility of hydrogen bonds among polar side chains, as well as between side chains and the protein backbone, make them crucial for stabilizing the three-dimensional folding of a protein.