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Updated: Jul 8, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Comparison of the efficiency of evolutionary change-based and side chain orientation-based fold recognition
Boris Vishnepolsky1, Grigol Managadze, Malak Pirtskhalava
1Institute of Molecular Biology and Biological Physics, Tbilisi 0160, Georgia.
Abstract:
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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