14656-09-8

Basic information

• Product Name: H-GLY-PHE-GLY-OH
• Synonyms: GLYCYL-L-PHENYLALANYL-GLYCINE;H-GLY-PHE-GLY-OH;Gly-Phe-Gly-OH≥ 98% (Assay)
• CAS NO: 14656-09-8
• Molecular Formula: C₁₃H₁₇N₃O₄
• Molecular Weight: 279.29
• Mol File: 14656-09-8.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 678.5°Cat760mmHg
• Flash Point: 364.1°C
• Appearance: /
• Density: 1.296g/cm³
• Vapor Pressure: 2.45E-19mmHg at 25°C
• Refractive Index: 1.576
• Storage Temp.: -15°C
• CAS DataBase Reference: H-GLY-PHE-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GLY-PHE-GLY-OH(14656-09-8)
• EPA Substance Registry System: H-GLY-PHE-GLY-OH(14656-09-8)

Safety Data

• Hazardous Substances Data: 14656-09-8(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C13H17N3O4/c14-7-11(17)16-10(13(20)15-8-12(18)19)6-9-4-2-1-3-5-9/h1-5,10H,6-8,14H2,(H,15,20)(H,16,17)(H,18,19)/t10-/m0/s1

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 35661-40-6 N-Fmoc L-Phe 
• 35737-10-1 N-Fmoc-β-alanine 

Downstream Products

• 58329-60-5 benzoyl-Gly-Phe-Gly 
• 50-00-0 formaldehyd 
• 124-38-9 carbon dioxide 
• 122-78-1 phenylacetaldehyde 

Relevant articles and documents

Fmoc-OPhth, the reagent of Fmoc protection

Fmoc-OSu has been widely used for Fmoc protection of amino groups, especially amino acids, in solid phase peptide synthesis. However, it has been recognized that Fmoc-βAla-OH is formed as a by-product via the Lossen rearrangement during the reaction. Since we reconfirmed the formation of Fmoc-βAla-OH during the preparation of Fmoc-AA-OH by Fmoc-OSu, Fmoc-OPhth was designed and synthesized as a new Fmoc reagent to avoid the formation of Fmoc-βAla-OH. Furthermore, Fmoc protection by Fmoc-OPhth and Fmoc-SPPS were evaluated. The various Fmoc-amino acids prepared by Fmoc-OPhth were carried out in good yields and these are applicable in Fmoc-SPPS.

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.