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dc.contributor.authorPapaloukas, C.en
dc.contributor.authorGranseth, E.en
dc.contributor.authorViklund, H.en
dc.contributor.authorElofsson, A.en
dc.date.accessioned2015-11-24T16:34:06Z-
dc.date.available2015-11-24T16:34:06Z-
dc.identifier.issn0961-8368-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7756-
dc.rightsDefault Licence-
dc.subjectmembrane proteinsen
dc.subjectcomputational analysis of protein structureen
dc.subjectprotein structure predictionen
dc.subjectmembrane-protein structureen
dc.subjecttopology predictionen
dc.subjectevolutionary informationen
dc.subjectcomplete genomesen
dc.subjectweb serveren
dc.subjectdatabaseen
dc.subjectaccuracyen
dc.subjectregionsen
dc.titleEstimating the length of transmembrane helices using Z-coordinate predictionsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1110/Ps.073036108-
heal.identifier.secondary<Go to ISI>://000252720700009-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1110/ps.073036108/asset/271_ftp.pdf?v=1&t=h1net3w3&s=5072b6158ad79f5d59928afa68197c4a99a2eae2-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2008-
heal.abstractZpred2 is an improved version of ZPRED, a predictor for the Z-coordinates of alpha-helical membrane proteins, that is, the distance of the residues from the center of the membrane. Using principal component analysis and a set of neural networks, Zpred2 analyzes data extracted from the amino acid sequence, the predicted topology, and evolutionary profiles. Zpred2 achieves an average accuracy error of 2.18 angstrom (2.17 angstrom when an independent test set is used), an improvement by 15% compared to the previous version. We show that this accuracy is sufficient to enable the predictions of helix lengths with a correlation coefficient of 0.41. As a comparison, two state-of-the-art HMM-based topology prediction methods manage to predict the helix lengths with a correlation coefficient of less than 0.1. In addition, we applied Zpred2 to two other problems, the re-entrant region identification and model validation. Re-entrants were able to be detected with a certain consistency, but not better than with previous approaches, while incorrect models as well as mispredicted helices of transmembrane proteins could be distinguished based on the Z-coordinate predictions.en
heal.journalNameProtein Scienceen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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