• DocumentCode
    2766961
  • Title

    Domain-domain interactions in obligate and non-obligate protein-protein interactions

  • Author

    Maleki, Mina ; Rueda, Luis

  • Author_Institution
    Sch. of Comput. Sci., Univ. of Windsor, Windsor, ON, Canada
  • fYear
    2011
  • fDate
    12-15 Nov. 2011
  • Firstpage
    907
  • Lastpage
    908
  • Abstract
    In this study, an analysis of protein-protein interactions (PPIs) that uses properties of domain-domain interactions (DDIs) present in the interface is discussed. The aim is to predict obligate and non-obligate complexes. The results show that support vector machines (SVM) classifier achieves much better prediction performance, even better than linear dimensionality reduction (LDR) schemes and aslo desolvation energy is better than interface area and composition for predicting transient and obligate complexes. Moreover, a visual and numerical analysis insight of the distribution of the DDIs in different complexes is shown that most homo-domain pairs are in obligate interactions.
  • Keywords
    biology computing; molecular biophysics; numerical analysis; proteins; support vector machines; desolvation energy; domain-domain interactions; homo-domain pairs; linear dimensionality reduction; numerical analysis; protein-protein interactions; support vector machine classifier; Accuracy; Amino acids; Bioinformatics; Protein engineering; Proteins; Support vector machines; Transient analysis; complex type prediction; domain-domain interaction; protein-protein interaction;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Bioinformatics and Biomedicine Workshops (BIBMW), 2011 IEEE International Conference on
  • Conference_Location
    Atlanta, GA
  • Print_ISBN
    978-1-4577-1612-6
  • Type

    conf

  • DOI
    10.1109/BIBMW.2011.6112498
  • Filename
    6112498