The complex formation in aqueous solution between the polyelectrolytes poly(lysine) and pectate was studied focusing on the conformational changes of the polysaccharidic moiety. The findings suggest that the pectate adopts a superhelical conformation around the α helix of the poly(l-lysine). A threshold value of the degree of polymerization of the pectate chain enabling the transition of the peptide was determined by chromatographic and circular dichroism methods. Conformational analysis results are in agreement with the experimental findings and support the superhelical topology of the polyelectrolyte poly(l-lysine)−pectate complex.

Paradossi, G., Chiessi, E., Malovikova, A. (2001). A Conformational Study of the Diastereomeric Poly(lysine) - Pectate complexes. MACROMOLECULES, 34, 8179-8186 [10.1021/ma010418x].

A Conformational Study of the Diastereomeric Poly(lysine) - Pectate complexes.

PARADOSSI, GAIO;CHIESSI, ESTER;
2001-01-01

Abstract

The complex formation in aqueous solution between the polyelectrolytes poly(lysine) and pectate was studied focusing on the conformational changes of the polysaccharidic moiety. The findings suggest that the pectate adopts a superhelical conformation around the α helix of the poly(l-lysine). A threshold value of the degree of polymerization of the pectate chain enabling the transition of the peptide was determined by chromatographic and circular dichroism methods. Conformational analysis results are in agreement with the experimental findings and support the superhelical topology of the polyelectrolyte poly(l-lysine)−pectate complex.
2001
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - CHIMICA FISICA
English
Con Impact Factor ISI
Paradossi, G., Chiessi, E., Malovikova, A. (2001). A Conformational Study of the Diastereomeric Poly(lysine) - Pectate complexes. MACROMOLECULES, 34, 8179-8186 [10.1021/ma010418x].
Paradossi, G; Chiessi, E; Malovikova, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/114626
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