Proteins such as enzymes perform their function by predominant
non-covalent bond interactions between transiently interacting units.
There is an impact on the overall structural topology of the protein,
albeit transient nature of such interactions, that enable proteins to
deactivate or activate. This aspect of the alteration of the structural
topology is studied by employing protein structural networks, which are
node-edge representative models of protein structure, reported as a
robust tool for capturing interactions between residues. Several methods
have been optimised to collect meaningful, functionally relevant
information by studying alteration of structural networks. In this
article, different methods of comparing protein structural networks are
employed, along with spectral decomposition of graphs to study the
subtle impact of protein-protein interactions. A detailed analysis of
the structural network of interacting partners is performed across a
dataset of around 900 pairs of bound complexes and corresponding unbound
protein structures. The variation in network parameters at, around and
far away from the interface are analysed. Finally, we present
interesting case studies, where an allosteric mechanism of structural
impact is understood from communication-path detection methods. The
results of this analysis are beneficial in understanding protein
stability, for future engineering and docking studies.