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dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorBirlirakis, N.en
dc.contributor.authorKarayannis, T.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorVitoux, B.en
dc.contributor.authorMarraud, M.en
dc.date.accessioned2015-11-24T16:39:11Z-
dc.date.available2015-11-24T16:39:11Z-
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8129-
dc.rightsDefault Licence-
dc.subjectmagnetic-resonance spectroscopyen
dc.subjectbound water-moleculesen
dc.subjectacetyl-l-prolineen
dc.subjectnmr-spectroscopyen
dc.subjectconformational-analysisen
dc.subjectprotein hydrationen
dc.subjectreverse turnsen
dc.subjecthydrogen-bonden
dc.subjectamino-acidsen
dc.subjectamide groupen
dc.titleHydration 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-Spectroscopyen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://A1992KF58100005-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1111/j.1432-1033.1992.tb17470.x/asset/j.1432-1033.1992.tb17470.x.pdf?v=1&t=h0e0lr50&s=20f1e58243db2baf6c09912c542b852d93777939-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1992-
heal.abstractSolvent-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.en
heal.publisherSpringer-Verlagen
heal.journalNameEuropean Journal of Biochemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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