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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