What type of bond primarily stabilizes tertiary protein structure?

The primary bonds that stabilize tertiary protein structure are not peptide bonds, but rather a combination of various interactions, including ionic bonds, hydrogen bonds, and disulfide bonds.

Tertiary structure refers to the overall three-dimensional shape of a protein that results from the folding and interactions of its amino acid side chains. While peptide bonds link amino acids together in the primary structure of proteins, they do not play a significant role in the tertiary structure. Instead, the tertiary structure is maintained by the intricate network of interactions among the side chains of the amino acids.

Ionic bonds occur between positively and negatively charged side chains, contributing to the stability of the folded protein. Hydrogen bonds form between polar side chains and help further stabilize the structure. Disulfide bonds, which are covalent links formed between the sulfur atoms of cysteine residues, provide additional stability, particularly in extracellular proteins.

Therefore, while peptide bonds are essential for forming the protein's primary sequence, they do not stabilize the tertiary structure to the same extent as ionic bonds, hydrogen bonds, and disulfide bonds do.