AspThrSerGly

AspThrSerGly, written as Asp-Thr-Ser-Gly, is a tetrapeptide composed of the amino acids aspartic acid (Asp), threonine (Thr), serine (Ser), and glycine (Gly). It can occur as a contiguous sequence within a larger protein or be studied as an isolated model peptide in experiments and peptide libraries. As a short motif, its significance is context-dependent rather than universal.

The chemical features of Asp-Thr-Ser-Gly influence its behavior. Asp provides a negative charge at physiological pH, Thr and Ser offer potential sites for phosphorylation, and Gly contributes minimal steric hindrance and increased local flexibility. Because Ser and Thr can be targets for serine/threonine kinases, such a motif might be considered in analyses of phosphorylation sites, motif discovery, or protein regulation, though the mere presence of these residues does not determine function by itself.

In research and proteomics, this tetrapeptide can serve as a test sequence or a component of smaller peptide libraries used to study kinase specificity, peptide–protein interactions, or mass spectrometry fragmentation patterns. It may also appear in natural proteins in various contexts, where surrounding residues and three-dimensional structure largely dictate its role.

Overall, Asp-Thr-Ser-Gly is best understood as a basic, context-dependent sequence rather than a universal functional motif. Its relevance emerges from its position within a larger protein and its interactions with cellular machinery. See also tetrapeptide, phosphorylation, and peptide motif.