Hydration of the Gly2 and Gly3 Peptide Oxygens of [Leu5]-Enkephalin in Aqueous-Solution as Revealed by the Combined Use of O-17-Nmr and Fourier-Transform Infrared-Spectroscopy (Journal article)
Gerothanassis, I. P./ Birlirakis, N./ Karayannis, T./ Sakarellos-Daitsiotis, M./ Sakarellos, C./ Vitoux, B./ Marraud, M.
Solvent-induced and temperature-induced O-17 chemical shifts of [O-17-Gly2, Leu5]-enkephalin and [O-17-Gly3, Leu5]-enkephalin and solvent-induced spectral modifications of the amide-I' stretching vibrations of [1-C-13-Gly2, Leu5]-enkephalin and [1-C-13-Gly2, Leu5]-enkephalin are reported and correlated with the spectroscopic characteristics of model amides. It is demonstrated that both Gly2 and Gly3 peptide oxygens are motionally equivalent and form solvation species which are essentially monohydrated in aqueous solution, contrary to several simple amides and model peptides in which water largely forms dihydrates. It is shown that the combined use of O-17-NMR and Fourier transform infrared is a unique methodology for studying the hydration state of specific peptide oxygens in peptide hormones.
|Institution and School/Department of submitter:||Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας|
|Keywords:||magnetic-resonance spectroscopy,bound water-molecules,acetyl-l-proline,nmr-spectroscopy,conformational-analysis,protein hydration,reverse turns,hydrogen-bond,amino-acids,amide group|
|Link:||<Go to ISI>://A1992KF58100005|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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