A systematic comparison with the Wild-Type (WT) of one-point mutants of bacteriophage
T4 lysozyme was carried out using as difference markers the topological parameters of the protein
contact networks corresponding to each crystallographic structure. The investigation concerned
changes at the resolution level of single residue along the protein sequence. The results were correlated
with (reported) changes in functional properties and (observed) changes in the information provided by
the energy dissipation algorithm of the “Turbine” software simulation tool. The critical factor leading
to significant difference among mutants and WT is in most cases associated to the sensitivity towards
mutation of relatively short windows in the amino acidic sequence not necessarily contiguous to the active site.
Keywords: Bacteriophage T4, lysozyme, network analysis, protein structure.
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