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DC Field | Value | Language |
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dc.contributor.author | Hemmerlin, C. | en |
dc.contributor.author | Du, A. P. C. | en |
dc.contributor.author | Elhilali, Z. | en |
dc.contributor.author | Moulia, A. | en |
dc.contributor.author | Tsikaris, V. | en |
dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
dc.contributor.author | Sakarellos, C. | en |
dc.contributor.author | Dotsika, E. | en |
dc.contributor.author | Tzioufas, A. G. | en |
dc.contributor.author | Moutsopoulos, H. M. | en |
dc.contributor.author | Cung, M. T. | en |
dc.date.accessioned | 2015-11-24T16:54:46Z | - |
dc.date.available | 2015-11-24T16:54:46Z | - |
dc.identifier.issn | 1387-1609 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10194 | - |
dc.rights | Default Licence | - |
dc.subject | sjogren's syndrome | en |
dc.subject | 2d-nmr | en |
dc.subject | noesy | en |
dc.subject | molecular modelling | en |
dc.subject | complementary peptide | en |
dc.subject | antigenic peptide | en |
dc.subject | specificity | en |
dc.subject | autoantibodies | en |
dc.title | Conformational study of the complementary peptide to a B-cell epitope of the La/SSB autoantigen | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.secondary | <Go to ISI>://000172445600003 | - |
heal.identifier.secondary | http://ac.els-cdn.com/S1387160901012968/1-s2.0-S1387160901012968-main.pdf?_tid=85ca55502d56d7ad55077c9a5804facd&acdnat=1333038488_3be191ed80fa91606bb5829414d0df88 | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 2001 | - |
heal.abstract | Starting from the 20-mer peptide 289-308, one of the experimentally characterized B-cell epitopes of the La/SSB autoantigen, the complementary peptide cpl(289-308), encoded by the complementary RNA was designed. The conformational properties of the cpl(289-308) were investigated in DMSO solution with the combined use of NMR data (vicinal coupling constants, NOE effects and temperature coefficient values), molecular modelling calculations of energy minimization and molecular dynamics. MD calculations led to a folded structure in which a betaI-turn, stabilized by the H-8 amide proton to the F-5 carbonyl hydrogen bond, was found for the F5P6S7H8 sequence, whereas two gamma -turns, centred around the E-15 and I-18 residues respectively, were found in the C-terminal part of the peptide. In the whole crown folded structure of the peptide, the Y-4, F-5, H-8, F-9 and F-10 aromatic side chains are situated on one side with the E-13, E-15, T-17 and Cc side chains on the other. This 3D structure resembles and could mimic the binding site of an antibody. (C) 2001 Academic des sciences/Editions scientifiques et medicales Elsevier SAS. | en |
heal.publisher | Elsevier | en |
heal.journalName | Comptes Rendus De L Academie Des Sciences Serie Ii Fascicule C-Chimie | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ |
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Hemmerlin-2001-Conformational study.pdf | 115.83 kB | Adobe PDF | View/Open Request a copy |
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