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.
basic_science · Level V
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- Record sourced from PubMed, PMID 21666270.
- Also identified by DOI 10.1093/bioinformatics/btr350 and PMC identifier 3137224.
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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/
Medical subject headings
- Computational Biology
- Protein Folding
- Proteins
- Sequence Alignment
- Sequence Analysis, Protein