This article examines how molecular structure and an aqueous environment affect amino acids' properties, suggesting implications for biochemistry.
L-α-amino acids are the fundamental building blocks of proteins and play a pivotal role in the biochemistry of living organisms. The behavior of these molecules in an aqueous solution – the primary medium for biological reactions – is contingent on their physicochemical properties, including molecular structure and dissociation constants (Ka). The objective of this article is to provide a comprehensive description of the chemical significance of amino acids in an aqueous environment. This encompasses their ionization states at varying pH, interactions with water molecules, environmental effects (e.g., ionic strength, temperature, the presence of other ions, and pressure), and the implications of these factors for the stability and biological function of the example peptides and proteins. The article also presents a discussion of contemporary experimental and computational methodologies employed in the study of the physicochemical properties of amino acids in an aqueous solution. It is imperative that these relationships are comprehended if advancements in the fields of drug design, protein engineering, and biotechnology are to be facilitated.
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Pająk et al. (2026) studied this question.
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