Conformation of Systemin, A Polypeptide Activator of Proteinase Inhibitor Synthesis in Plants

摘要

An 18-amino acid polypeptide systemin was synthesized by the solid-phase method and its conformation was studied by circular dichroism spectroscopy. The peptide in solution is a mixture of random coil structure with #beta#-sheet and #beta#-turn motifs as has been previously suggested with NMR spectra. Free zone capillary electrophoresis analysis proved purity and chemical stability of systemin at different pH.