Protein-protein interactions are crucial for many physiological processes, including enzyme catalysis and inhibition, immune response, and endocytosis. The rate of association and dissociation of these protein complexes is important for characterizing their formation and stability, as well as understanding their broader cellular role. However, experimental determination of these association and dissociation constants is not always possible or accurate, as protein-protein complexes pass through transient states that are difficult to capture experimentally. As such, computational techniques for determining protein-protein association and dissociation rate constants are useful and necessary. However, methods such as conventional molecular dynamics (MD) and Brownian dynamics (BD) are unable to reach the necessary detail or time scale for accurate predictions on their own. This talk will detail our approach to calculating association and dissociation rate constants with a multiscale MD/BD simulation approach, as well as possible ways to expand the results of this work to even higher scales of simulation.

The video of this presentation is available here.