PLoS ONE (Jun 2008)

SP5: improving protein fold recognition by using torsion angle profiles and profile-based gap penalty model.

  • Wei Zhang,
  • Song Liu,
  • Yaoqi Zhou

DOI
https://doi.org/10.1371/journal.pone.0002325
Journal volume & issue
Vol. 3, no. 6
p. e2325

Abstract

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How to recognize the structural fold of a protein is one of the challenges in protein structure prediction. We have developed a series of single (non-consensus) methods (SPARKS, SP(2), SP(3), SP(4)) that are based on weighted matching of two to four sequence and structure-based profiles. There is a robust improvement of the accuracy and sensitivity of fold recognition as the number of matching profiles increases. Here, we introduce a new profile-profile comparison term based on real-value dihedral torsion angles. Together with updated real-value solvent accessibility profile and a new variable gap-penalty model based on fractional power of insertion/deletion profiles, the new method (SP(5)) leads to a robust improvement over previous SP method. There is a 2% absolute increase (5% relative improvement) in alignment accuracy over SP(4) based on two independent benchmarks. Moreover, SP(5) makes 7% absolute increase (22% relative improvement) in success rate of recognizing correct structural folds, and 32% relative improvement in model accuracy of models within the same fold in Lindahl benchmark. In addition, modeling accuracy of top-1 ranked models is improved by 12% over SP(4) for the difficult targets in CASP 7 test set. These results highlight the importance of harnessing predicted structural properties in challenging remote-homolog recognition. The SP(5) server is available at http://sparks.informatics.iupui.edu.