Surface-facilitated trapping by active sites: From catalysts to viruses.

Trapping by active sites on surfaces plays important roles in various chemical and biological processes, including catalysis, enzymatic reactions, and viral entry into host cells. However, the mechanisms of these processes remain not well understood, mostly because the existing theoretical descriptions are not fully accounting for the role of the surfaces. Here, we present a theoretical investigation on the dynamics of surface-assisted trapping by specific active sites.

Role of Intrinsically Disordered Regions in Acceleration of Protein-Protein Association.

Although intrinsically disordered proteins and intrinsically disordered regions (IDRs) in folded proteins are not able to form stable structures, it is known that they play critically important roles in various biological processes. However, despite multiple studies, the molecular mechanisms of their functions remain not fully understood. In this work, we theoretically investigate the role of IDRs in acceleration of protein-protein association processes.

Theoretical Investigation of the Mechanisms of ERK2 Enzymatic Catalysis.

ERK2 are protein kinases that during the enzymatic catalysis, in contrast to traditional enzymes, utilize additional interactions with substrates outside of the active sites. It is widely believed that these docking interactions outside of the enzymatic pockets enhance the specificity of these proteins. However, the molecular mechanisms of how the docking interactions affect the catalysis remain not well understood.