03557nas a2200157 4500008004100000245008600041210006900127260000800196300001200204490000700216520299400223100001803217700001503235700003303250856011603283 2019 eng d00aExploring energy profiles of protein-protein interactions (PPIs) Using DFT method0 aExploring energy profiles of proteinprotein interactions PPIs Us cJUN a670-6770 v163 a

Background: Large-scale energy landscape characterization of protein-protein interactions (PPIs) is important to understand the interaction mechanism and protein-protein docking methods. The experimental methods for detecting energy landscapes are tedious and the existing computational methods require longer simulation time.

Objective: The objective of the present work is to ascertain the energy profiles at the interface regions in a rapid manner to analyze the energy landscape of protein-protein interactions

Methods: The atomic coordinates obtained from the X-ray and NMR spectroscopy data are considered as inputs to compute cumulative energy profiles for experimentally validated protein-protein complexes. The energies computed by the program were comparable to the standard molecular dynamics simulations.

Results: The PPI Profiler not only enables rapid generation of energy profiles but also facilitates the detection of hot spot residue atoms involved therein.

Conclusion: The hotspot residues and their computed energies matched with the experimentally determined hot spot residues and their energies which correlated well by employing the MM/GBSA method. The proposed method can be employed to scan entire proteomes across species at an atomic level to study the key PPI interactions.

1 aBapat, Sanket1 aVyas, Renu1 aKarthikeyan, Muthukumarasamy uhttps://library.ncl.res.in/content/exploring-energy-profiles-protein-protein-interactions-ppis-using-dft-method