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.
|Titolo:||THERMODYNAMIC AND PROTON NMR STUDY OF PROTON COMPLEX-FORMATION OF HISTIDINE-CONTAINING CYCLODIPEPTIDES IN AQUEOUS-SOLUTION|
|Data di pubblicazione:||1992|
|Appare nelle tipologie:||1.1 Articolo in rivista|