Analyzing mechanisms and microscopic reversibility of self-assembly.

We use computer simulations to investigate self-assembly in a system of model chaperonin proteins, and in an Ising lattice gas. We discuss the mechanisms responsible for rapid and efficient assembly in these systems, and we use measurements of dynamical activity and assembly progress to compare their propensities for kinetic trapping. We use the analytic solution of a simple minimal model to illustrate the key features associated with such trapping, paying particular attention to the number of ways that particles can misbind. We discuss the relevance of our results for the design and control of self-assembly in general.