Blocking and single-point mutations of aminoacids in biological enzymes through Protein Residue Networks (PRN) and graph-theory representations. Analysis of local and non-local spreading effects.

Graph-theory and network analysis have become one of the main analytical and computational frameworks to analyze connectivity, topology and function in biological enzymes. In this work, we analyze the effect of blocking specific amino acid residues within protein's globular structures in order to quantify the local and non-local effects that such mutations and blockings may have on the main network connectivity. To achieve this, we consider the SARS-CoV2 main protease Mpro in apo structure and Mpro complexed with Boceprevir, one the main known inhibitors of this enzyme. We compute main network centralities for both the apo and complexed structures and then we target a set of relevant aminoacid residues for blocking. We analyze then the local and non-local effects of blocking such residues in terms of connectivity within the global apo and complexed structures