The prediction of protein structure from its amino acid sequence is one of the most prominent problems in computational biology. The biological function of a protein depends on its tertiary structure which is determined by its amino acid sequence via the process of protein folding. We propose a novel fold recognition method for protein tertiary structure prediction based on a hidden Markov model and 3D coordinates of amino acid residues. The method introduces states based on the basis vectors in Bravais cubic lattices to learn the path of amino acids of the proteins of each fold. Three hidden Markov models are considered based on simple cubic, body-centered cubic (BCC) and face-centered cubic (FCC) lattices. A 10-fold cross validation was performed on a set of 42 fold SCOP dataset. The proposed composite methodology is compared to fold recognition methods which have HMM as base of their algorithms having approaches on only amino acid sequence or secondary structure. The accuracy of proposed model based on face-centered cubic lattices is quite better in comparison with SAM, 3-HMM optimized and Markov chain optimized in overall experiment. The huge data of 3D space help the model to have greater performance in comparison to methods which use only primary structures or only secondary structures.
Proteins are essential for the biological processes in the human body. They can only perform their functions when they fold into their tertiary structure. We propose a novel fold recognition method for protein tertiary structure prediction based on a hidden Markov model and 3D coordinates of amino acid residues in 3D space. The method introduces states based on the basis vectors in Bravais cubic lattice to recognise the fold of proteins. The accuracy of proposed model is quite better in comparison with SAM, 3-HMM optimised and Markov chain in overall experiment.
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