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Comparison of the efficiency of evolutionary change-based and side chain orientation-based fold recognition potentials

Comparison of the efficiency of evolutionary change-based and side chain orientation-based fold recognition potentials

Proteins 71(4): 1863-1878

The present article describes residue level knowledge based potential SORDIS. SORDIS incorporates the information on side-chain orientation in relation to hydrophobic core centres, distance of residue from the globule centre and secondary structure. SORDIS has been tested and compared with widespread evolutionary change-based substitution matrices (BLOSUM, PAM, GONNET, Johnson-Overington, BLAJ, HSDM, and STROMA) in fold recognition experiments within the zone of weak sequence similarity (<16%). The obtained results show that the lower is the amino acid similarity between homologous pairs the higher is the performance of SORDIS in comparison with the potentials, based on the information about the evolutionary changes. Therefore, we propose that the employment of SORDIS in fold recognition can be useful.

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Accession: 030647761

Download citation: RISBibTeXText

PMID: 18175309

DOI: 10.1002/prot.21871

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