Protein structural alignment is an indispensable tool used for many different studies in bioinformatics. Most structural alignment algorithms assume that the structural units of two similar proteins will align sequentially. This assumption may not be true for all similar proteins and as a result, proteins with similar structure but with permuted sequence arrangement are often missed. We present a solution to the problem based on an approximation algorithm that finds a sequence-order independent structural alignment that is close to optimal. We first exhaustively fragment two proteins and calculate a novel similarity score between all possible aligned fragment pairs. We treat each aligned fragment pair as a vertex on a graph. Vertices are connected by an edge if there are intra residue sequence conflicts. We regard the realignment of the fragment pairs as a special case of the maximum-weight independent set problem and solve this computationally intensive problem approximately by iteratively solving relaxations of an appropriate integer programming formulation. The resulting structural alignment is sequence order independent. Our method is insensitive to gaps, insertions/deletions, and circular permutations. © Springer-Verlag Berlin Heidelberg 2007.
CITATION STYLE
Dundas, J., Binkowski, T. A., DasGupta, B., & Liang, J. (2007). Topology independent protein structural alignment. In Lecture Notes in Computer Science (including subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) (Vol. 4645 LNBI, pp. 171–182). Springer Verlag. https://doi.org/10.1007/978-3-540-74126-8_16
Mendeley helps you to discover research relevant for your work.