CD and NMR techniques have been used to study, in acetonitrile solution, the ion-complexing capability of Cyclolinopeptide A (CLA). The relevant conformational features of the equimolar Ba2+/CLA are that the backbone contains all trans peptide bonds , a type I beta turn, and a gamma turn. The global shape of the compelx can be described as a bowl with the polar side hosting the ion Ba2+and the convex side predominantly apolar.

Ion binding of cyclolinopeptide A: An NMR and CD conformational study / Tancredi, T.; Benedetti, E.; Grimaldi, M.; Pedone, C.; Rossi, Filomena; Saviano, M.; Temussi, P. A.; Zanotti, G.. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 31:(1991), pp. 761-767.

Ion binding of cyclolinopeptide A: An NMR and CD conformational study

ROSSI, FILOMENA;
1991

Abstract

CD and NMR techniques have been used to study, in acetonitrile solution, the ion-complexing capability of Cyclolinopeptide A (CLA). The relevant conformational features of the equimolar Ba2+/CLA are that the backbone contains all trans peptide bonds , a type I beta turn, and a gamma turn. The global shape of the compelx can be described as a bowl with the polar side hosting the ion Ba2+and the convex side predominantly apolar.
1991
Ion binding of cyclolinopeptide A: An NMR and CD conformational study / Tancredi, T.; Benedetti, E.; Grimaldi, M.; Pedone, C.; Rossi, Filomena; Saviano, M.; Temussi, P. A.; Zanotti, G.. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 31:(1991), pp. 761-767.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/457886
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