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dc.contributor.authorTzaphlidou, M.en
dc.contributor.authorHardcastle, R. A.en
dc.date.accessioned2015-11-24T19:40:31Z-
dc.date.available2015-11-24T19:40:31Z-
dc.identifier.issn0020-7101-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24366-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subject*Collagenen
dc.subjectCollagen Diseases/*diagnosisen
dc.subject*Computersen
dc.subjectHumansen
dc.subjectMicroscopy, Electronen
dc.subjectProtein Conformationen
dc.titleA computer method for the comparison or the quantitative similarity between normal and abnormal collagen or between sequence data and experimental dataen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/6724728-
heal.identifier.secondaryhttp://ac.els-cdn.com/0020710184900230/1-s2.0-0020710184900230-main.pdf?_tid=8316de2560d1839f758171f2667e6c80&acdnat=1333106209_a6ff0b610e77e432f38f63dd48ed0c7d-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1984-
heal.abstractIn this paper, a method is described to correlate collagen structural data obtained by electron microscopy with chemical sequence data, or to compare two experimental sets of data. In this respect, collagen provides a valuable model system, firstly for studying the chemical basis of ultrastructure and the mechanisms of various treatments on a protein, and secondly for detecting and locating the alterations in collagen fibril structure produced by a collagen disorder.en
heal.journalNameInt J Biomed Computen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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