Collect. Czech. Chem. Commun.
1999, 64, 553-558
https://doi.org/10.1135/cccc19990553
Conformation of Systemin, a Polypeptide Activator of Proteinase Inhibitor Synthesis in Plants
Piotr Muchaa, Agnieszka Szyka, Piotr Rekowskia, Gotfryd Kupryszewskia, Genowefa Slósarekb and Jan Barciszewskic,*
a Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland
b Department of Molecular Biophysics, Institute of Physics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
c Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12, 61-704 Poznań, Poland
Abstract
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 β-sheet and β-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.
Keywords: Systemin conformation; Circular dichroism; Free zone capillary electrophoresis; Peptide conformation; Peptides.
