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[[File:Bronsted_character_of_ionizing_groups_in_proteins.png|thumb|upright=1.8|Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues]]
The common natural forms of amino acids have a [[zwitterionic]] structure, with {{chem2|\sNH3+}} ({{chem2|\sNH2+\s}} in the case of proline) and {{chem2|\sCO2-}} functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome.
In aqueous solution at pH close to neutrality, amino acids exist as [[zwitterion]]s, i.e. as dipolar ions with both {{chem2|NH3+}} and {{chem2|CO2-}} in charged states, so the overall structure is {{chem2|NH3+\sCHR\sCO2-}}. At [[Acid–base homeostasis|physiological pH]] the so-called "neutral forms" {{chem2|\sNH2\sCHR\sCO2H}} are not present to any measurable degree. Although the two charges in the zwitterion structure add up to zero it is misleading to call a species with a net charge of zero "uncharged".

Translations:Amino acid/27/en - Revision history

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