作者: Kazuhisa Fujimoto , Masaoki Kajino , Masahiko Inouye
关键词: Chemistry 、 Protein structure 、 Stereochemistry 、 Alpha helix 、 Molecular conformation 、 α helical 、 Crystallography 、 Circular dichroism 、 Peptide
摘要: A series of cross-linking agents varying rigidity and length were designed to stabilize helical structures in short peptides then synthesized. The sequences the employed this study each include two X residues (X=Dap, Dab, Orn, Lys) at i/i+4, i/i+7, or i/i+11 positions provide sites for cross-linking. These subjected reaction with synthesized agents, content resulting cross-linked analyzed detail by circular dichroism. For peptide classes we found combinations suitable construction stable up >95 % helicity 5 degrees C. Our method could also be applied biologically related seen native proteins such as Rev.