In the context of crowded cellular environment, one of the important challenges is to elucidate how proteins distinguish their native partners from a wide variety of non-interactors. The increasing availability of experimentally determined protein-protein complexes provides an opportunity to investigate significant preferences in protein-protein interaction. We systematically explored the shape complementarity of the interacting proteins using available binary hetero complexes from the Protein Data Bank. The results showed that protein shape characteristics and the corresponding intermolecular energy landscape, sampled by systematic free docking protocol, can discriminate the non-interacting proteins. The number of minima on the energy landscape of known interactors, as well as the clustering patterns of the energy basins, are different from those of the non-native protein ligands. The findings provide an insight into the fundamental properties of protein recognition. The results can be also used to generate more adequate sets of protein-protein complexes for knowledge-based modeling.

Standing out in the crowd: Native protein partners are distinct from the non-native ones in protein-protein interactions

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.