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Backbone dihedral angles prediction servers for protein early-stage structure prediction

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Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Three-dimensional protein structure prediction is an important task in science at the intersection of biology, chemistry, and informatics, and it is crucial for determining the protein function. In the two-stage protein folding model, based on an early- and late-stage intermediates, we propose to use state-of-the-art secondary structure prediction servers for backbone dihedral angles prediction and devise an early-stage structure. Early-stage structures are used as a starting point for protein folding simulations, and any errors in this stage affect the final predictions. We have shown that modern secondary structure prediction servers could increase the accuracy of early-stage predictions compared to previously reported models.
Rocznik
Strony
art. no. 20190034
Opis fizyczny
Bibliogr. 35 poz., rys., tab.
Twórcy
  • Institute of Informatics, Silesian University of Technology, Akademicka 16, Gliwice, Poland
  • Institute of Informatics, Silesian University of Technology, Akademicka 16, Gliwice, Poland
  • Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Kraków, Poland
Bibliografia
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  • [11] Gadzała M, Dułak D, Kalinowska B, Baster Z, Bryliński M, Konieczny L, et al. The aqueous environment as an active participant in the protein folding process. J Mol Graph Modell 2019;87:227-39.
  • [12] Heffernan R, Yang Y, Paliwal KK, Zhou Y. Capturing non-local interactions by long short-term memory bidirectional recurrent neural networks for improving prediction of protein secondary structure, backbone angles, contact numbers and solvent accessibility. Bioinformatics 2017;33:2842-9.
  • [13] Fang C, Shang Y, Xu D. MUFOLD-SS: new deep inception-inside-inception networks for protein secondary structure prediction. Proteins 2018;86:592-8.
  • [14] Kalinowska B, Alejster P, Sałapa K, Baster Z, Roterman I. Hypothetical in silico model of the early-stage intermediate in protein folding. J Mol Model 2013;19:4259-69.
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Uwagi
Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2020).
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-d18739e6-ba6b-4a9d-a0d2-e4fa3e46109c
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