Conformation of systemin, a polypeptide activator of proteinase inhibitor synthesis in plants

Authors
Mucha, P Szyk, A Rekowski, P Kupryszewski, G Slosarek, G Barciszewski, J
Citation
P. Mucha et al., Conformation of systemin, a polypeptide activator of proteinase inhibitor synthesis in plants, COLL CZECH, 64(3), 1999, pp. 553-558
Citations number
11
Categorie Soggetti
Chemistry
Journal title
COLLECTION OF CZECHOSLOVAK CHEMICAL COMMUNICATIONS
ISSN journal
00100765 → ACNP
Volume
64
Issue
3
Year of publication
1999
Pages
553 - 558
Database
ISI
SICI code
0010-0765(199903)64:3<553:COSAPA>2.0.ZU;2-C
Abstract
An 18-amino acid polypeptide systemin was synthesized by the solid-phase me thod and its conformation was studied by circular dichroism spectroscopy. T he peptide in solution is a mixture of random coil structure with beta-shee t and beta-turn motifs as has been previously suggested with NMR spectra. F ree zone capillary electrophoresis analysis proved purity and chemical stab ility of systemin at different pH.