• DocumentCode
    1153613
  • Title

    Improved K-means clustering algorithm for exploring local protein sequence motifs representing common structural property

  • Author

    Zhong, Wei ; Altun, Gulsah ; Harrison, Robert ; Tai, Phang C. ; Pan, Yi

  • Author_Institution
    Comput. Sci. Dept., Georgia State Univ., Atlanta, GA, USA
  • Volume
    4
  • Issue
    3
  • fYear
    2005
  • Firstpage
    255
  • Lastpage
    265
  • Abstract
    Information about local protein sequence motifs is very important to the analysis of biologically significant conserved regions of protein sequences. These conserved regions can potentially determine the diverse conformation and activities of proteins. In this work, recurring sequence motifs of proteins are explored with an improved K-means clustering algorithm on a new dataset. The structural similarity of these recurring sequence clusters to produce sequence motifs is studied in order to evaluate the relationship between sequence motifs and their structures. To the best of our knowledge, the dataset used by our research is the most updated dataset among similar studies for sequence motifs. A new greedy initialization method for the K-means algorithm is proposed to improve traditional K-means clustering techniques. The new initialization method tries to choose suitable initial points, which are well separated and have the potential to form high-quality clusters. Our experiments indicate that the improved K-means algorithm satisfactorily increases the percentage of sequence segments belonging to clusters with high structural similarity. Careful comparison of sequence motifs obtained by the improved and traditional algorithms also suggests that the improved K-means clustering algorithm may discover some relatively weak and subtle sequence motifs, which are undetectable by the traditional K-means algorithms. Many biochemical tests reported in the literature show that these sequence motifs are biologically meaningful. Experimental results also indicate that the improved K-means algorithm generates more detailed sequence motifs representing common structures than previous research. Furthermore, these motifs are universally conserved sequence patterns across protein families, overcoming some weak points of other popular sequence motifs. The satisfactory result of the experiment suggests that this new K-means algorithm may be applied to other areas of bioinformatics resea- - rch in order to explore the underlying relationships between data samples more effectively.
  • Keywords
    biology computing; greedy algorithms; molecular biophysics; molecular configurations; proteins; statistical analysis; bioinformatics; common structural property; greedy initialization method; improved K-means clustering algorithm; local protein sequence motifs; protein activities; protein conformation; structural similarity; Bioinformatics; Biology; Cancer; Clustering algorithms; Computer science; Diseases; Information science; Protein sequence; Sequences; Testing; protein structure; sequence motif; Algorithms; Amino Acid Motifs; Amino Acid Sequence; Cluster Analysis; Conserved Sequence; Molecular Sequence Data; Pattern Recognition, Automated; Protein Conformation; Proteins; Sequence Alignment; Sequence Analysis, Protein; Sequence Homology, Amino Acid;
  • fLanguage
    English
  • Journal_Title
    NanoBioscience, IEEE Transactions on
  • Publisher
    ieee
  • ISSN
    1536-1241
  • Type

    jour

  • DOI
    10.1109/TNB.2005.853667
  • Filename
    1501844