21835-35-8

Usage

Uses

Used in Biochemistry and Pharmaceutical Research:
H-VAL-GLY-GLY-OH is used as a research compound for studying the properties and interactions of amino acids in various biochemical processes. Its unique structure allows scientists to explore its potential in modulating biological activities and developing new therapeutic agents.
Used in Drug Development:
H-VAL-GLY-GLY-OH is used as a building block in the development of peptide-based drugs. Its specific amino acid sequence may contribute to the design of novel therapeutic agents with targeted biological activities, such as modulating immune responses or treating specific diseases.
Used in Peptide-based Materials:
H-VAL-GLY-GLY-OH is used as a component in the synthesis of peptide-based materials, which have potential applications in tissue engineering, drug delivery systems, and other biomedical applications. Its incorporation into these materials can enhance their properties, such as biocompatibility, stability, and functionality.
Used in Cosmetics and Personal Care Products:
H-VAL-GLY-GLY-OH is used as an active ingredient in cosmetics and personal care products for its potential skin conditioning and moisturizing properties. Its presence in these products may contribute to improved skin health and appearance.
Used in Food and Nutritional Supplements:
H-VAL-GLY-GLY-OH is used as a nutritional supplement to support muscle metabolism and tissue repair. Its presence in dietary supplements may help athletes and individuals with specific health conditions to maintain optimal muscle function and recovery.
Used in Agricultural Applications:
H-VAL-GLY-GLY-OH is used in agricultural applications to enhance plant growth and improve crop yields. Its potential role in plant metabolism and stress resistance may contribute to increased productivity and resilience in various crops.

InChI:InChI=1/C9H17N3O4/c1-5(2)8(10)9(16)12-3-6(13)11-4-7(14)15/h5,8H,3-4,10H2,1-2H3,(H,11,13)(H,12,16)(H,14,15)

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 68858-20-8 Fmoc-Val-OH 

Downstream Products

• 264285-84-9 N-[4-[4-(Acetylaminobenzyl)phenyl]carbamoyl]valyl-glycyl-glycine 

Relevant academic research and scientific papers

Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy

Several approaches for utilizing dipolar recoupling solid-state NMR (ssNMR) techniques to determine local structure at high resolution in peptides and proteins have been developed. However, many of these techniques measure only one torsion angle or are accurate for only certain classes of secondary structure. Additionally, the efficiency with which these dipolar recoupling experiments suppress the deleterious effects of chemical shift anisotropy (CSA) at high magnetic field strengths varies. Dipolar recoupling with a windowless sequence (DRAWS) has proven to be an effective pulse sequence for exciting double-quantum (DQ) coherences between adjacent carbonyl carbons along the peptide backbone. By allowing this DQ coherence to evolve, it is possible to measure the relative orientations of the CSA tensors and subsequently use this information to determine the Ramachandran torsion angles φ and ψ. Here, we explore the accuracies of the assumptions made in interpreting DQ-DRAWS data and demonstrate their fidelity in measuring torsion angles corresponding to a variety of secondary structures irrespective of hydrogen-bonding patterns. It is shown how a simple choice of isotopic labels and experimental conditions allows accurate measurement of backbone secondary structures without any prior knowledge. This approach is considerably more sensitive for determining structure in helices and has comparable accuracy for β-sheet and extended conformations relative to other methods. We also illustrate the ability of DQ-DRAWS to distinguish between structures in heterogeneous samples.