Final answer:
Lysine can form an ionic bond with aspartic acid due to the electrostatic attraction between their opposite charges, stabilizing protein structures.
Step-by-step explanation:
The side chain of lysine could interact with the side chain of aspartic acid using a(n) ionic bond. Lysine has a positively charged side chain at physiological pH, while aspartic acid has a negatively charged carboxylate group. The electrostatic attraction between these opposite charges forms an ionic bond, which is a common type of interaction in proteins, helping to stabilize their structure.
The side chain of lysine could interact with the side chain of aspartic acid using a(n) ionic bond. Ionic bonds result from electrostatic attractions between positively and negatively charged side chains of amino acids. The mutual attraction between an aspartic acid carboxylate ion and a lysine ammonium ion helps to maintain a particular folded area of a protein.