20807-28-7

Basic information

• Product Name: H-ALA-PHE-GLY-OH
• Synonyms: H-ALA-PHE-GLY-OH
• CAS NO: 20807-28-7
• Molecular Formula: C14H19N3O4
• Molecular Weight: 293.32
• Mol File: 20807-28-7.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 665.6±55.0 °C(Predicted)
• Appearance: /
• Density: 1.263±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.30±0.10(Predicted)
• CAS DataBase Reference: H-ALA-PHE-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-ALA-PHE-GLY-OH(20807-28-7)
• EPA Substance Registry System: H-ALA-PHE-GLY-OH(20807-28-7)

Safety Data

• Hazardous Substances Data: 20807-28-7(Hazardous Substances Data)

Usage

General Description

H-ALA-PHE-GLY-OH is a peptide composed of the amino acids alanine (ALA), phenylalanine (PHE), and glycine (GLY), connected in that order. Alanine is a nonpolar, neutral amino acid, phenylalanine is an aromatic amino acid, and glycine is the simplest of all amino acids. When combined in a specific sequence, these amino acids can create a peptide with potential biological activity. The "OH" at the end of the chemical name indicates that this peptide is terminated with a carboxylic acid group, making it a C-terminal amino acid sequence. H-ALA-PHE-GLY-OH may be used in the study of peptide chemistry, protein interactions, and as a building block in the creation of peptides for various research and medical applications.

Upstream product

• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 35661-40-6 N-Fmoc L-Phe 
• 7148-74-5 2-Bromopropionyl chloride 

Relevant articles and documents

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.