Abstract
An active area of research in bioinformatics is finding structural similarity of proteins by alignment. Among many methods, the popular one is to find the similarity based on statistical features. This method involves gathering information from the complex biomolecule structure and obtaining the best alignment by maximizing the number of matched features. In this paper, after reviewing statistical models for matching the structural biomolecule, it is shown that local alignment based on the Delaunay tetrahedralization (DT) can be used for Bayesian alignment of proteins. In this method, we use DT to add a priori structural information of protein in the Bayesian methodology. We demonstrate that this method shows advantages over competing methods in achieving a global alignment of proteins, accelerating the convergence rate and improving the parameter estimates.
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