Protein Secondary Structures Prediction based on Evolutionary Computation Alfonso E. Márquez Chamorro School of Engineering Pablo de Olavide University Seville, Spain Federico Divina School of Engineering Pablo de Olavide University Seville, Spain Jesús S. Aguilar-Ruiz School of Engineering Pablo de Olavide University Seville, Spain fdiv@upo.es aguilar@upo.es amarcha@upo.es ABSTRACT In this paper we propose an approach based on evolutionary computation for the prediction of secondary protein structure motifs. The prediction model consists of a set of rules that predict both the beginning and the end of the regions corresponding to a secondary structure state conformation ( -helix or -strand). The prediction is based on a set of specific amino acid physicalchemical properties. In addition we also propose a statistical study regarding the propensities of each pair of amino acids in capping regions of -helix and -strand. Experimental results con rm the validity of our proposal.1 peptide chains ( -strands), which are held together with hydrogen bonds in a zig-zag, constitute a -sheet motif. The lamellar structure formed proportionate exibility but no elasticity. The adjacent chains of a -sheet can be targeted in the same direction (parallel -sheet) or opposite direction (antiparallel -sheet). Several methods were applied to the PSSP
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Protein secondary structures prediction based on evolutionary computation
Chamorro, Alfonso E. Márquez; Divina, Federico; Aguilar-Ruiz, Jesús S.
Follow ACM SIGAPP Applied Computing Review
, Volume 11 (4)
Association for Computing Machinery – Dec 1, 2011
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