PFRES

  • Authors:
  • Ke Chen;Lukasz Kurgan

  • Affiliations:
  • -;-

  • Venue:
  • Bioinformatics
  • Year:
  • 2007

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Abstract

Motivation: The number of protein families has been estimated to be as small as 1000. Recent study shows that the growth in discovery of novel structures that are deposited into PDB and the related rate of increase of SCOP categories are slowing down. This indicates that the protein structure space will be soon covered and thus we may be able to derive most of remaining structures by using the known folding patterns. Present tertiary structure prediction methods behave well when a homologous structure is predicted, but give poorer results when no homologous templates are available. At the same time, some proteins that share twilight-zone sequence identity can form similar folds. Therefore, determination of structural similarity without sequence similarity would be beneficial for prediction of tertiary structures. Results: The proposed PFRES method for automated protein fold classification from low identity ( Availability: The method is freely available from the authors upon request. Contact: lkurgan@ece.ualberta.ca Supplementary information: Supplementary data are available at Bioinformatics online.