Abstract
Actin polymerization time courses can exhibit rich nonequilibrium dynamics that have not yet been accurately described by simplified rate equations. Sophisticated stochastic simulations and elaborate recursion schemes have been used to model the nonequilibrium dynamics resulting from the hydrolysis and subsequent exchange of the nucleotide bound within the actin molecules. In this work, we use a truncation approach to derive a set of readily accessible deterministic rate equations which are significantly simpler than previous attempts at such modeling. These equations may be incorporated into whole-cell motility models which otherwise quickly become computationally inaccessible if polymerization of individual actin filaments is stochastically simulated within a virtual cell. Our equations accurately predict the relative concentrations of both monomeric and polymerized actin in differing nucleotide hydrolysis states throughout entire polymerization time courses nucleated via seed filaments. We extend our model to include the effects of capping protein. We also detail how our rate-equation method may be used to extract key parameters from experimental data.