Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/14444
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dc.contributor.authorIconomidou, V. A.en
dc.contributor.authorChryssikos, D. G.en
dc.contributor.authorGionis, V.en
dc.contributor.authorPavlidis, M. A.en
dc.contributor.authorPaipetis, A.en
dc.contributor.authorHamodrakas, S. J.en
dc.date.accessioned2015-11-24T17:38:07Z-
dc.date.available2015-11-24T17:38:07Z-
dc.identifier.issn1047-8477-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/14444-
dc.rightsDefault Licence-
dc.subjectatr-ir spectroscopyen
dc.subjectfish eggshell (chorion)en
dc.subjectft-raman spectroscopyen
dc.subjecthelicoidal architectureen
dc.subjectbeta-pleated sheeten
dc.subjectscanning microscopyen
dc.subjecttransform infrared-spectroscopyen
dc.subjectwater h2o solutionsen
dc.subjectamide-ien
dc.subjectlaser-ramanen
dc.subjectpeptide compoundsen
dc.subjectabsorption-bandsen
dc.subjectsalmo-gairdnerien
dc.subjectpolypeptidesen
dc.subjecteggshellen
dc.subjectspectraen
dc.titleSecondary structure of chorion proteins of the teleostean fish Dentex dentex by ATR FT-IR and FT-Raman spectroscopyen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1006/jsbi.2000.4307-
heal.identifier.secondary<Go to ISI>://000167116800004-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1047847700943077/1-s2.0-S1047847700943077-main.pdf?_tid=a9278872219fa2ee7c0e1a1097215792&acdnat=1339672881_a4e508728bd3e8696ce207affe8a626a-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικώνel
heal.publicationDate2000-
heal.abstractFT-Raman spectroscopy and ATR-IR spectroscopy were applied to study the secondary structure of the eggshell (chorion) proteins of the teleostean fish Dentex dentex. Raman and IR spectra clearly indicate an abundance of antiparallel P-pleated sheet conformation in chorion proteins. This finding is further supported by analysis of the vibrational data by regression techniques and deconvolution procedures. Thus, the common morphological characteristics of D, dentex, Salmo gairdneri, and other teleostean fish chorions may be explained on the basis of common secondary structure features of their constituent proteins. A detailed understanding of the interactions that dictate the self-assembly of fish chorion proteins to form the fish eggshell awaits determination of aminoacid sequences, (C) 2000 Academic Press.en
heal.publisherElsevieren
heal.journalNameJ Struct Biolen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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