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DC Field | Value | Language |
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dc.contributor.author | Iconomidou, V. A. | en |
dc.contributor.author | Chryssikos, D. G. | en |
dc.contributor.author | Gionis, V. | en |
dc.contributor.author | Pavlidis, M. A. | en |
dc.contributor.author | Paipetis, A. | en |
dc.contributor.author | Hamodrakas, S. J. | en |
dc.date.accessioned | 2015-11-24T17:38:07Z | - |
dc.date.available | 2015-11-24T17:38:07Z | - |
dc.identifier.issn | 1047-8477 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/14444 | - |
dc.rights | Default Licence | - |
dc.subject | atr-ir spectroscopy | en |
dc.subject | fish eggshell (chorion) | en |
dc.subject | ft-raman spectroscopy | en |
dc.subject | helicoidal architecture | en |
dc.subject | beta-pleated sheet | en |
dc.subject | scanning microscopy | en |
dc.subject | transform infrared-spectroscopy | en |
dc.subject | water h2o solutions | en |
dc.subject | amide-i | en |
dc.subject | laser-raman | en |
dc.subject | peptide compounds | en |
dc.subject | absorption-bands | en |
dc.subject | salmo-gairdneri | en |
dc.subject | polypeptides | en |
dc.subject | eggshell | en |
dc.subject | spectra | en |
dc.title | Secondary structure of chorion proteins of the teleostean fish Dentex dentex by ATR FT-IR and FT-Raman spectroscopy | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.primary | DOI 10.1006/jsbi.2000.4307 | - |
heal.identifier.secondary | <Go to ISI>://000167116800004 | - |
heal.identifier.secondary | http://ac.els-cdn.com/S1047847700943077/1-s2.0-S1047847700943077-main.pdf?_tid=a9278872219fa2ee7c0e1a1097215792&acdnat=1339672881_a4e508728bd3e8696ce207affe8a626a | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικών | el |
heal.publicationDate | 2000 | - |
heal.abstract | FT-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.publisher | Elsevier | en |
heal.journalName | J Struct Biol | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) |
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File | Description | Size | Format | |
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Iconomidou-2000-Secondary structure.pdf | 182.66 kB | Adobe PDF | View/Open Request a copy |
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