Final answer:
The forces that contribute to a protein's tertiary structure include hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages. These interactions stabilize the folding pattern of a protein and determine its three-dimensional structure.
Step-by-step explanation:
The forces that help a protein fold into its tertiary shape are largely hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages. These interactions stabilize the three-dimensional folding pattern of a protein by facilitating the proper arrangement of the protein's side chains. For example, hydrophobic interactions occur when hydrophobic (water-repelling) amino acid side chains come together in the protein's interior, away from water. Ionic bonding involves the attraction between positively and negatively charged amino acid side chains. Hydrogen bonding occurs when polar amino acid side chains form weak bonds with each other. Disulfide linkages are covalent bonds that form between the sulfur atoms of cysteine amino acids. Overall, these forces contribute to the stability and functionality of proteins.