• DocumentCode
    2504632
  • Title

    DomSVR: Domain Boundary Prediction with Support Vector Regression and Evolutionary Information

  • Author

    Chen, Peng ; Liu, Chunmei ; Burge, Legand ; Mahmood, Mohammad ; Southerland, William ; Gloster, Clay

  • Author_Institution
    Dept. of Syst. & Comput. Sci., Howard Univ., Washington, DC, USA
  • fYear
    2009
  • fDate
    11-13 June 2009
  • Firstpage
    1
  • Lastpage
    5
  • Abstract
    Protein domains are autonomous folding units and are fundamental structural and functional units of proteins. Protein domain boundaries are helpful to the classification of proteins and understanding the evolutions, structures and functions of proteins. In this paper, we propose a support vector regression based method to locate residues at protein domain boundaries with a combination of evolutionary information including sequence profiles, predicted secondary structures, predicted relative solvent accessibility, and profiles from HSSP items. Our proposed model achieved an average sensitivity of ~37% and an average specificity of ~77% on domain boundary identification on our dataset of multi-domain proteins and showed better predictive performance than previous domain identification models.
  • Keywords
    bioinformatics; evolutionary computation; molecular biophysics; proteins; regression analysis; support vector machines; DomSVR; autonomous folding units; domain boundary prediction; evolutionary information; multidomain protein; protein classification; protein domain; protein structure; secondary structure; sequence profile; solvent accessibility; support vector regression; Amino acids; Biochemistry; Computer science; Databases; Mathematics; Neural networks; Predictive models; Protein engineering; Sequences; Solvents;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Bioinformatics and Biomedical Engineering , 2009. ICBBE 2009. 3rd International Conference on
  • Conference_Location
    Beijing
  • Print_ISBN
    978-1-4244-2901-1
  • Electronic_ISBN
    978-1-4244-2902-8
  • Type

    conf

  • DOI
    10.1109/ICBBE.2009.5162660
  • Filename
    5162660