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  • Autor
    • Doncheva, Nadezhda
    • Klein, Karsten
    • Morris, John
    • Wybrow, Michael
    • Domingues, Francisco
    • Albrecht, Mario
  • TitelIntegrative visual analysis of protein sequence mutations
  • Volltext
  • DOI10.1186/1753-6561-8-S2-S2
  • Persistent Identifier
  • Erschienen inBMC Proceedings
  • Band8
  • Erscheinungsjahr2014
  • HeftSuppl 2
  • LicenceCC-BY
  • ISSN1753-6561
  • ZugriffsrechteCC-BY
  • Download Statistik134
  • Peer ReviewNein
  • AbstractBACKGROUND:An important aspect of studying the relationship between protein sequence, structure and function is the molecular characterization of the effect of protein mutations. To understand the functional impact of amino acid changes, the multiple biological properties of protein residues have to be considered together.RESULTS:Here, we present a novel visual approach for analyzing residue mutations. It combines different biological visualizations and integrates them with molecular data derived from external resources. To show various aspects of the biological information on different scales, our approach includes one-dimensional sequence views, three-dimensional protein structure views and two-dimensional views of residue interaction networks as well as aggregated views. The views are linked tightly and synchronized to reduce the cognitive load of the user when switching between them. In particular, the protein mutations are mapped onto the views together with further functional and structural information. We also assess the impact of individual amino acid changes by the detailed analysis and visualization of the involved residue interactions. We demonstrate the effectiveness of our approach and the developed software on the data provided for the BioVis 2013 data contest.CONCLUSIONS:Our visual approach and software greatly facilitate the integrative and interactive analysis of protein mutations based on complementary visualizations. The different data views offered to the user are enriched with information about molecular properties of amino acid residues and further biological knowledge.