Acidic amino acids such as aspartic acid and glutamic acid have a negatively charged side chain due to the presence of carboxyl (COOH) functional groups. These carboxyl groups can ionize in an aqueous (water-based) medium by donating a hydrogen ion (H+), resulting in the formation of a carboxylate anion (COO-).
This negative charge on the carboxylate group makes the amino acid side chain polar and hydrophilic (water-loving). The polar nature of these amino acids allows them to interact with other polar molecules and ions in solution, facilitating important molecular interactions and bio-molecular processes.
Furthermore, this negatively charged property of acidic amino acids allows them to act as acid-base catalysts in enzymatic reactions. They can donate or accept protons, playing a crucial role in various metabolic pathways.
Overall, the negatively charged nature of acidic amino acids is a result of the ionization of carboxyl functional groups, contributing to their unique biochemical properties and functions in biological systems.
WHY acidic amino acids are polar negativily charged
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