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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9572
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dc.contributor.authorBiris, N.en
dc.contributor.authorStavrakoudis, A.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorMikros, E.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:50:08Z-
dc.date.available2015-11-24T16:50:08Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9572-
dc.rightsDefault Licence-
dc.subjectarginine ionic interactionsen
dc.subjectaspartic acid ionic interactionsen
dc.subjectfibrinogen inhibitoren
dc.subjecthydrogen bondsen
dc.subjectnmren
dc.subjectpeptide foldingen
dc.subjectrgd peptideen
dc.subjectslow conformational exchangeen
dc.subjectcasei dihydrofolate-reductaseen
dc.subjectnuclear-magnetic-resonanceen
dc.subjectside-chain conformationsen
dc.subjectamino-acid sequenceen
dc.subjectmolecular-dynamicsen
dc.subjectcarboxylate groupsen
dc.subjectarginineen
dc.subjectrgden
dc.subjectnmren
dc.subjectguanidiniumen
dc.titleThe Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSOen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1002/Bip.10335-
heal.identifier.secondary<Go to ISI>://000182620800006-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.10335/asset/10335_ftp.pdf?v=1&t=h0e0jil1&s=610cf5404c7616cce6f19e1f1bda9ebb1deeb075-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2003-
heal.abstractAccording to general belief the conformational information on short linear peptides in solution derived at ambient temperature from NMR spectrometry represents a population-weighted average over all members of an ensemble of rapidly interconverting conformations. Usually the search for discrete conformations is concentrated at low temperatures especially when sharp NMR resonances are detected at room temperature. Using the peptide Ac-RGD-NH2 (Ac-Arg-Gly-Asp-NH2, Ac: acetyl) as a model system and following a new approach, we have been able to demonstrate that short linear peptides can adopt discrete conformational states in DMSO-d(6), (DMSO: dimethylsulfoxide) which vary in a way critically dependent on the reconstitution conditions used before their dissolution in DMSO-d(6),. The conformers are stabilized by intramolecular hydrogen bonds, which persist at high temperatures and undergo a very slow exchange with their extended structures in the NMR chemical shift time scale. The reported findings provide clear evidence for the occurrence of solvent-induced conformational exchange and point to DMSO as a valuable medium for folding studies of short linear peptides. (C) 2003 Wiley Periodicals, Inc.en
heal.publisherWileyen
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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