Glycine is the simplest of the twenty standard amino acids, distinguished by a side chain consisting of a single hydrogen atom, which makes it the smallest and least sterically hindered amino acid. This compact structure allows glycine to occupy positions in protein folds where larger residues cannot fit, giving it …
Glycine is the simplest of the twenty standard amino acids, distinguished by a side chain consisting of a single hydrogen atom, which makes it the smallest and least sterically hindered amino acid. This compact structure allows glycine to occupy positions in protein folds where larger residues cannot fit, giving it a special role in the structure of proteins such as collagen, where it appears at regular intervals. Beyond its structural contributions, glycine participates in numerous biochemical pathways: it is a building block for the synthesis of proteins, and it contributes to the production of creatine, the porphyrin ring of hemoglobin, glutathione, and nucleic acids. In the central nervous system, glycine also functions as an inhibitory neurotransmitter. Because it is involved in so many metabolic and physiological processes, glycine is of broad interest in biochemistry, nutrition, and physiology. Research published in this journal relevant to glycine includes a study on early glycine supplementation and its effect on adrenal catecholamine secretion in an experimental model, reflecting interest in the amino acid's physiological roles. As an open-access journal devoted to amino acids, this publication addresses the chemistry, biology, and applications of these fundamental molecules. This page collects peer-reviewed scholarship relevant to glycine and its functions.
12 peer-reviewed articles, ranked by relevance. Each links to its DOI.
The 12 articles above have been cited 85 times in the scholarly literature. Citation data via OpenAlex and Crossref, updated Jun 2026.
A sample of recent works citing this journal's research on Glycine, linking to each citing work.