CLePAPS: Fast Pair Alignment of Protein Structures Based on Conformational Letters

Details CLePAPS: Fast Pair Alignment of Protein Structures Based on Conformational Letters CLePAPS: Fast Pair Alignment of Protein Structures Based on Conformational Letters

2007-10-31

arxiv.org/abs/0710.5817v1

Biology

Quantitative Biology

Quantitative Methods

1 figure

Scientific paper

Fast, efficient and reliable algorithms for pairwise alignment of protein structures are in ever increasing demand for analyzing the rapidly growing data of protein structures. CLePAPS is a tool developed for this purpose. It distinguishes itself from other existing algorithms by the use of conformational letters, which are discretized states of 3D segmental structural states. A letter corresponds to a cluster of combinations of the three angles formed by C_alpha pseudobonds of four contiguous residues. A substitution matrix called CLESUM is available to measure similarity between any two such letters. CLePAPS regards an aligned fragment pair (AFP) as an ungapped string pair with a high sum of pairwise CLESUM scores. Using CLESUM scores as the similarity measure, CLePAPS searches for AFPs by simple string comparison. The transformation which best superimposes a highly similar AFP can be used to superimpose the structure pairs under comparison. A highly scored AFP which is consistent with several other AFPs determines an initial alignment. CLePAPS then joins consistent AFPs guided by their similarity scores to extend the alignment by several `zoom-in' iteration steps. A follow-up refinement produces the final alignment. CLePAPS does not implement dynamic programming. The utility of CLePAPS is tested on various protein structure pairs.

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