Glycine is the simplest amino acid, with the chemical formula H2NCH2COOH and a side chain consisting of a single hydrogen atom. Its lack of a stereocenter makes it the only proteinogenic amino acid that is achiral, and its small size allows it to occupy tightly packed or sharply turned regions of protein structure, …
Glycine is the simplest amino acid, with the chemical formula H2NCH2COOH and a side chain consisting of a single hydrogen atom. Its lack of a stereocenter makes it the only proteinogenic amino acid that is achiral, and its small size allows it to occupy tightly packed or sharply turned regions of protein structure, contributing to the periodic glycine repeats of collagen. As a zwitterion at physiological pH, glycine bears both protonated amine and deprotonated carboxylate groups, giving it buffering capacity and high water solubility. Metabolically it participates in one-carbon and amino acid metabolism, in the synthesis of heme, purines, creatine, and glutathione, and as an inhibitory neurotransmitter in the central nervous system. In synthetic and analytical chemistry glycine serves as a building block in peptide synthesis, a ligand in coordination chemistry, and a reactant in Maillard and other carbonyl reactions during food processing. Its simplicity also makes it a model substrate for studying reaction mechanisms and supplementation effects in biological systems. New Developments in Chemistry publishes peer-reviewed research touching on glycine and related amino acids, including peptide synthesis methods, amino acid supplementation studies, and the biochemistry of metabolic regulation.
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.