Affiliations: [a] Department of CSE, University of California, Riverside, CA 92521, United States. [email protected] | [b] Department of Computational Engineering and Science, McMaster University, Hamilton, Ontario, Canada. [email protected] | [c] Department of CSE, BUET, Dhaka-1205, Bangladesh. [email protected] | [d] AℓEDA Group, Department of CSE, BUET, ECE Building, West Palasi, Dhaka-1205, Bangladesh. [email protected]
Correspondence:
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Address for correspondence: Department of CSE, BUET, ECE Building West Palasi, Dhaka-1205, Bangladesh Dhaka-1205, Bangladesh.
Abstract: Predicting the secondary structure of a protein using a lattice model is one of the most studied computational problems in bioinformatics. Here the secondary structure or three dimensional structure of a protein is predicted from its amino acid sequence. The secondary structure refers to the local sub-structures of a protein. Simplified energy models have been proposed in the literature on the basis of interaction of amino acid residues in proteins. We focus on a well researched model known as the Hydrophobic-Polar (HP) energy model. In this paper, we propose the hexagonal prism lattice with diagonals that can overcome the problems of other lattice structures, e.g., parity problem. We give two approximation algorithms for protein folding on this lattice using HP model. Our first algorithm leads us to a similar structure of helix structure that is commonly found in a protein structure. This motivates us to propose the next algorithm with a better approximation ratio. Finally, we analyze the algorithms on the basis of intensity of the chemical forces along the different types of edges of hexagonal prism lattice with diagonals.
