https://www.selleckchem.com/pr....oducts/pci-34051.htm
The hydrophobic diphenylalanine peptide crystal is known to be unusually stiff, with an experimental Young's modulus in the range of 19-27 GPa. Here it is shown by means of density functional theory calculations that phenylalanine-leucine, leucine-phenylalanine, alanine-valine, valine-alanine and valine-valine hydrophobic dipeptide crystals are also unusually stiff, with Young's moduli in the range of 19.7-33.3 GPa. To further our understanding of the origin of that unusual stiffness, a linear correlation is established between Young'
Like
Comment
Share
