What drives the formation of the tertiary structure in proteins?

The formation of the tertiary structure in proteins is primarily driven by hydrophobic interactions and interactions between the R groups (side chains) of amino acids. During the folding process, the hydrophobic side chains tend to move away from the aqueous environment, seeking to minimize contact with water. This creates a core of non-polar residues, while polar and charged residues often remain on the exterior to interact with the surrounding water.

Additionally, the specific types of interactions that occur between the R groups, including hydrogen bonds, ionic bonds, and van der Waals forces, contribute to the stabilization of the protein's three-dimensional shape. These interactions allow for intricate folding that determines the protein's functionality, making the interplay of the R groups vital in achieving the unique tertiary structure necessary for the protein's biological role.

While hydrogen bonds can play a role in stabilizing the tertiary structure, they are not the primary driving force; rather, they are one of several interactions involved. The sequence of amino acids is critical for overall structure and function, but it is the interactions between those amino acid side chains that ultimately drive the formation of the tertiary structure. Covalent bonds can provide stability, for example through disulfide bonds, but they are not the main factor driving the formation