Add time:08/03/2019         Source:sciencedirect.com

The molecular conformation of achatin-II neutral form (H-Gly-Phe-Ala-Asp-OH), an endogenous peptide from the Achatina fulica ganglia, was elucidated by X-ray crystal analysis. The molecule takes an extended β-pleated structure stabilized by 5 intermolecular hydrogen bonds with the antiparallely arranged molecules. This is in contrast with the turn conformation of a neuroactive achatin-I (H-Gly-d-Phe-Ala-Asp-OH) [(1992) FEBS Lett. 276, 95–97]. The conformational comparison of both of the molecules makes clear the structural role which d-Phe residue of achatin-I plays in forming a definite active form.

We also recommend Trading Suppliers and Manufacturers of H-GLY-ASP-GLY-OH (cas 10517-27-8). Pls Click Website Link as below: cas 10517-27-8 suppliers