Motivation: A useful approach to evaluate protein structure and quickly visualize crucial physicochemical interactions related to protein function is to construct Residue Interactions Networks (RINs). By using this application of graphs theory, the amino acid residues constitute the nodes, and the edges represent their interactions with other structural elements. Although several tools that construct RINs are available, many of them do not compare RINs from distinct protein structures. This comparison can give valuable insights into the understanding of conformational changes and the effects of amino acid substitutions in protein structure and function. With that in mind, we present CoRINs (Comparator of Residue Interaction Networks), a software tool that extensively compares RINs. The program has an accessible and user-friendly web interface, which summarizes the differences in several network parameters using interactive plots and tables. As a usage example of CoRINs, we compared RINs from conformers of two cancer-associated proteins. Availability: The program is available at https://github.com/LasisUFRN/CoRINs. Keywords: RINs, physical-chemical interactions, conformational variation, protein structure analysis. Competing Interest Statement The authors have declared no competing interest. Footnotes * https://github.com/LasisUFRN/CoRINs...

CoRINs: A tool to compare residue interaction networks from homologous proteins and conformers

10.1101/2020.06.29.178541