Amino acids are classified as acidic, basic, or neutral based on the relative number of amino and carboxyl groups in their molecules. Equal numbers result in neutrality, more amino groups make them basic, and more carboxyl groups make them acidic.
How are amino acids classified as acidic, basic, or neutral, and what determines their classification?
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Amino acids are classified as acidic, basic, or neutral based on their side chain properties. Those with acidic side chains (e.g., aspartic acid, glutamic acid) can donate protons and are considered acidic. Amino acids with basic side chains (e.g., lysine, arginine) can accept protons and are classified as basic. Amino acids with non-ionizable side chains (e.g., glycine, alanine) are considered neutral. The classification depends on the functional groups within the side chains and their ability to donate, accept, or remain non-reactive to protons, influencing the overall charge of the amino acid at physiological pH and their role in biochemical reactions.