A thermodynamic and H-1 NMR study of proton complex formation in aqueous solution of some L-histidine-containing cyclic L-dipeptides has been carried out. The enthalpic and entropic changes associated with protonation of the cyclodipeptides, obtained by potentiometric and calorimetric measurements, together with the H-1 NMR data and NOESY experiments, enable the role played by non-covalent interactions in proton complex formation to be assessed. In addition, a comparison with c(Glys-His) permits the influence of side-chain residues on the conformation of protonated species to be observed.

A thermodynamic and H-1 NMR study of proton complex formation in aqueous solution of some L-histidine-containing cyclic L-dipeptides has been carried out. The enthalpic and entropic changes associated with protonation of the cyclodipeptides, obtained by potentiometric and calorimetric measurements, together with the H-1 NMR data and NOESY experiments, enable the role played by non-covalent interactions in proton complex formation to be assessed. In addition, a comparison with c(Glys-His) permits the influence of side-chain residues on the conformation of protonated species to be observed.

THERMODYNAMIC AND H-1-NMR STUDY OF PROTON COMPLEX-FORMATION OF HISTIDINE-CONTAINING CYCLODIPEPTIDES IN AQUEOUS-SOLUTION

ARENA, Giuseppe;SCIOTTO, Domenico;RIZZARELLI E.
1992-01-01

Abstract

A thermodynamic and H-1 NMR study of proton complex formation in aqueous solution of some L-histidine-containing cyclic L-dipeptides has been carried out. The enthalpic and entropic changes associated with protonation of the cyclodipeptides, obtained by potentiometric and calorimetric measurements, together with the H-1 NMR data and NOESY experiments, enable the role played by non-covalent interactions in proton complex formation to be assessed. In addition, a comparison with c(Glys-His) permits the influence of side-chain residues on the conformation of protonated species to be observed.
1992
A thermodynamic and H-1 NMR study of proton complex formation in aqueous solution of some L-histidine-containing cyclic L-dipeptides has been carried out. The enthalpic and entropic changes associated with protonation of the cyclodipeptides, obtained by potentiometric and calorimetric measurements, together with the H-1 NMR data and NOESY experiments, enable the role played by non-covalent interactions in proton complex formation to be assessed. In addition, a comparison with c(Glys-His) permits the influence of side-chain residues on the conformation of protonated species to be observed.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.11769/46851
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