In the expansive landscape of bioch Val-L-Ser, L- Bioaustralis Fine Chemicals emistry, understanding the fundamental building blocks of proteins is essential. Among these, the val ser dipeptide, scientifically known as Leu-Val-Ser | C14H27N3O5 | CID 9858135 - PubChem valylserine, serves as a compelling subject for those interested in the structural nuances of amino Val-Asp-Ser| C12H21N3O7 | CID 60163825 - structure, chemical names, physical and chemical properties, classification, patents, literature, acid sequences. As an organic compound derived from two amino acids, this molecule provides a clear window into how specific residues like valine and serine interact to form stable, functional units.
Structural Fundamentals and Chemical Identity
At its core, Val-Ser is a dipeptide composed of the amino acid L-valine and L-serine. When researchers examine the molecular formula: C8H16N2O4, they are looking at a compound with an average mass of approximately 204.226 Da. This molecule is often discussed alongside its isomer, Ser-Val is a dipeptide, which consists of the same constituents but in a different sequence.
The ch Ser-Val - 51782-06-0 emical versatility of these structures is notable. For example, Ser-Val contains reactive groups such as a primary amine at the N-terminus, a carboxylic acid at the C-terminus, and a hydroxyl group from the serine side chain. This arrangement makes it a frequent subject of study in labs focusing on dipeptide interactions and their roles as metabolites. Because valylserine is a dipeptide resulting from protein catabolism, it is frequently identified in metabolic screenings.
Contextualizing Dipeptides in Research
The study of these molecules often extends into larger, more complex chains. While a peptide of this size is relatively simple, it provides the foundation for understanding longer sequences. For instance, researchers may compare the properties of Val-Ser to a tripeptide like Leu-Val-Ser is a tripeptide, or even more specific sequences such as Val-Ser-Ala.
In professional research environments, L-Val-L-Ser (valylserine) is acknowledged as one of approximately 400 possible dipeptides found in nature. It is often contrasted with other compounds like Val-Asp-Ser, illustrating the diversity of chemical properties that emerge when different amino acids are linked via peptide bonds. Whether one is investigating Val-Ser-Ala or exploring the structural requirements for protein synthesis, these small molecules remain a cornerstone of chemical inquiry.
Broader Peptide Applications
Beyond the simple Val-Ser linkage, the scientific literature frequently highlights more complex synthetic sequences. A prominent example is Val-Gly-Ser-Glu (NSC 350591), which is a synthetic peptide composed of four amino acids. This specific sequence, often cataloged under Val-Gly-Ser-Glu CAS 61756-22-7, is characterized as an eosi Showing metabocard for Valylserine (HMDB0029136) nophilic chemotactic tetrapeptide.
ValGly refers to adipeptidecomposed of the amino acids valine and glycine, which is involved in the formation of various chelate products during peptide Read moreSimilarly, investigations into other sequences like H-Val-Leu-Ser-OH peptide demonstrate the precision required when synthesizing these chains for model studies. In these contexts, the Val-Gly-Ser-Glu molecule acts as a critical reference point for researchers analyzing how specific residues influence biological activity. Furthermore, a comprehensive overview of the tripeptide Val-Phe-Ser often provides the necessary methodology for those Description: A tripeptide representing the Fas-C terminus that specifically blocks the interaction of Fap1 with Fas; increases apoptosis sensitivity and Read more looking to understand how these chains are constructed and analyzed in a laboratory setting.
Technical Insights for Enthusiasts
For those curious about the mechanics of protein assembly, it is worth noting that is a dipeptide compound that can be used for protein synthesis. The interaction between Val and Ser residues is a standard model for understanding the stability of peptide bonds. Whether you are reviewing data on Val-Gly-Ser-Glu or examining the physical properties of a simple dipeptide, the focus remains on ho This peptide corresponds to residues 2099-2104 of the laminin alpha1 chain. It has been shown to modulate tumor invasion, metastasis and angiogenesis.Read more w these sequences are organized.
By analyzing these components, we gain a deeper appreciation for the molecular precision that governs biological systems. From the structural formula of Val-Ser to the functional complexity of larger peptides, these compounds continue to be vital tools for scientific exploration and understanding the fundamental nature of chemical bonds.