Final answer:
Protein folding involves the primary interactions of ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces.
Step-by-step explanation:
The forces involved in a protein folding into its final conformation are primarily ionic, hydrogen, disulfide linkages, and dispersion forces. Ionic bonding refers to the electrostatic attraction between positively and negatively charged side chains of amino acids. Hydrogen bonding forms between highly electronegative atoms like oxygen or nitrogen and hydrogen atoms attached to other oxygen or nitrogen atoms. Disulfide linkages are covalent bonds formed between two sulfur atoms in different parts of the protein, while dispersion forces are weak attractions between temporary dipoles in nonpolar amino acid side chains.