20274-89-9 Usage
Description
Glycyl-glycyl-L-valine, also known as (S)-2-(2-(2-Aminoacetamido)acetamido)-4-methylbutanoic Acid, is a tripeptide consisting of three amino acids: glycine, glycine, and L-valine. It is a type of peptide that has unique properties and potential applications in various fields due to its specific structure and composition.
Uses
Used in Pharmaceutical Industry:
Glycyl-glycyl-L-valine is used as a research compound for studying its properties and potential applications in the pharmaceutical industry. Its unique structure and composition make it a valuable tool for understanding the interactions between peptides and other biological molecules, which can lead to the development of new drugs and therapies.
Used in Biomedical Research:
In the field of biomedical research, Glycyl-glycyl-L-valine is used as a model compound to investigate the properties of peptides and their interactions with biological systems. This can help researchers gain insights into the mechanisms of various diseases and develop targeted treatments.
Used in Cosmetics Industry:
Glycyl-glycyl-L-valine may also find applications in the cosmetics industry, where it can be used as an active ingredient in skincare products. Its properties may contribute to skin hydration, anti-aging effects, or other beneficial outcomes for skin health.
Used in Food Industry:
In the food industry, Glycyl-glycyl-L-valine could potentially be used as a flavor enhancer or as a component in the development of new food products. Its unique taste and properties may provide novel sensory experiences for consumers.
Used in Agricultural Applications:
Glycyl-glycyl-L-valine may also have potential applications in agriculture, where it could be used to improve the nutritional content of crops or to enhance the growth and development of plants.
Overall, Glycyl-glycyl-L-valine is a versatile tripeptide with a wide range of potential applications across various industries. Its unique structure and properties make it a valuable compound for research and development, with the potential to contribute to advancements in healthcare, cosmetics, food, and agriculture.
Check Digit Verification of cas no
The CAS Registry Mumber 20274-89-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,0,2,7 and 4 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 20274-89:
(7*2)+(6*0)+(5*2)+(4*7)+(3*4)+(2*8)+(1*9)=89
89 % 10 = 9
So 20274-89-9 is a valid CAS Registry Number.
InChI:InChI=1/C9H17N3O4/c1-5(2)8(9(15)16)12-7(14)4-11-6(13)3-10/h5,8H,3-4,10H2,1-2H3,(H,11,13)(H,12,14)(H,15,16)/t8-/m0/s1
20274-89-9Relevant articles and documents
Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy
Mehta, Manish A.,Eddy, Matthew T.,McNeill, Seth A.,Mills, Frank D.,Long, Joanna R.
, p. 2202 - 2212 (2008/09/18)
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.
