Template-based multi-domain protein structure assembling method

Abstract

The invention discloses a template-based multi-domain protein structure assembling method. The method comprises the steps of firstly, comparing domain proteins once by utilizing a protein structure comparison tool TM-align according to the structures of the domain proteins, and finding out an optimal template from a multi-domain protein database; secondly, obtaining a rotation and translation matrix by utilizing a Kabsch method, overlapping the domain proteins to the template, and performing translation and rotation operations on the domain proteins, thereby enabling a distance between the domain proteins to be equal to a minimum allowed distance; thirdly, performing adjustment by performing random translation and rotation on an assembled structure, and measuring the quality of the assembled structure by utilizing a conflict factor between the domain proteins, an interactive atom quantity and a moving range of the assembled structure relative to the template; and in an assembling process, assembling the adjacent domain proteins in sequence, fixing the assembled structures, and when all the structures are assembled, outputting a final assembling result. The template-based multi-domain protein structure assembling method provided by the invention is relatively high in prediction precision.

Description

technical field [0001] The invention relates to the fields of biological informatics, intelligent optimization and computer application, and in particular to a template-based multi-domain protein structure assembly method. Background technique [0002] Large-scale proteins are usually composed of multiple independently folded domain proteins, and the determination of the structure of multi-domain proteins can greatly promote the progress of biological research. Domain proteins usually have a compact three-dimensional structure and specific biological functions, and the same domain protein may have different structures. In addition, the single-domain three-dimensional structure of many multi-domain proteins has been determined by X-ray diffraction, nuclear magnetic resonance and computer prediction. Therefore, it is an important step to obtain the structure of the corresponding multi-domain protein based on the structure of the single-domain protein, and a necessary link to ...

AI Technical Summary

Problems solved by technology

However, due to the lack of template guidance in the above method, the assembly direction of the domain protein cannot be determined during assembly, resulting in low prediction accuracy

[0004] Therefore, existing multi-domain protein structure assembly methods are deficient in prediction accuracy and need to be improved

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