Protein-protein interactions (PPIs) are crucial for understanding the signaling and disease mechanisms in a cell. In the present work, we have developed a new approach to explore the energy landscape of protein-protein interactions by employing a rapid modified DFT-D approach using the atomic coordinates obtained from X-ray and NMR spectroscopy data. The distance energy plots of contact residues in the interacting regions of several experimentally validated protein-protein complexes were computed to generate energy landscapes. Cumulative energy profiles of protein-protein complexes were generated for observing trends in the context of geometry (parallel, terminal), surface areas (large, medium, small) and interacting partners (homomer, heteromer).

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Registered

2016-03-08