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      Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of query and corresponding native properties of templates.

      Bioinformatics
      Algorithms, Computational Biology, methods, Models, Molecular, Protein Folding, Protein Structure, Secondary, Proteins, chemistry, Sequence Alignment, Sequence Analysis, Protein

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          Abstract

          In recent years, development of a single-method fold-recognition server lags behind consensus and multiple template techniques. However, a good consensus prediction relies on the accuracy of individual methods. This article reports our efforts to further improve a single-method fold recognition technique called SPARKS by changing the alignment scoring function and incorporating the SPINE-X techniques that make improved prediction of secondary structure, backbone torsion angle and solvent accessible surface area. The new method called SPARKS-X was tested with the SALIGN benchmark for alignment accuracy, Lindahl and SCOP benchmarks for fold recognition, and CASP 9 blind test for structure prediction. The method is compared to several state-of-the-art techniques such as HHPRED and BoostThreader. Results show that SPARKS-X is one of the best single-method fold recognition techniques. We further note that incorporating multiple templates and refinement in model building will likely further improve SPARKS-X. The method is available as a SPARKS-X server at http://sparks.informatics.iupui.edu/

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          Author and article information

          Journal
          21666270
          3137224
          10.1093/bioinformatics/btr350

          Chemistry
          Algorithms,Computational Biology,methods,Models, Molecular,Protein Folding,Protein Structure, Secondary,Proteins,chemistry,Sequence Alignment,Sequence Analysis, Protein

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