The stability of the tertiary structure is maintained by various interactions:
Hydrogen bonds: Formed between polar side chains and the polypeptide backbone. Disulfide bridges: Covalent bonds formed between cysteine residues. Hydrophobic interactions: Nonpolar side chains tend to cluster together, avoiding water. Ionic interactions: Attraction between oppositely charged side chains.
These interactions collectively contribute to the stability and proper folding of the enzyme, ensuring its catalytic efficiency.
