• DocumentCode
    1755412
  • Title

    A New Strategy for Protein Interface Identification Using Manifold Learning Method

  • Author

    Bing Wang ; De-Shuang Huang ; Changjun Jiang

  • Author_Institution
    Adv. Res. Inst. of Intell. Sensing Network, Tongji Univ., Shanghai, China
  • Volume
    13
  • Issue
    2
  • fYear
    2014
  • fDate
    41791
  • Firstpage
    118
  • Lastpage
    123
  • Abstract
    Protein interactions play vital roles in biological processes. The study for protein interface will allow people to elucidate the mechanism of protein interaction. However, a large portion of protein interface data is incorrectly collected in current studies. In this paper, a novel strategy of dataset reconstruction using manifold learning method has been proposed for dealing with the noises in the interaction interface data whose definition is based on the residue distances among the different chains within protein complexes. Three support vector machine-based predictors are constructed using different protein features to identify the functional sites involved in the formation of protein interface. The experimental results achieved in this work demonstrate that our strategy can remove noises, and therefore improve the ability for identification of protein interfaces with 77.8% accuracy.
  • Keywords
    biology computing; learning (artificial intelligence); proteins; support vector machines; dataset reconstruction; functional sites; manifold learning method; noise removal; protein complexes; protein features; protein interactions; protein interface data; protein interface identification; residue distances; support vector machine-based predictors; Amino acids; Learning systems; Manifolds; Nanobioscience; Proteins; Support vector machines; Vectors; Denoising strategy; manifold learning; protein interaction; protein interface identification; support vector machine;
  • fLanguage
    English
  • Journal_Title
    NanoBioscience, IEEE Transactions on
  • Publisher
    ieee
  • ISSN
    1536-1241
  • Type

    jour

  • DOI
    10.1109/TNB.2014.2316997
  • Filename
    6803991