 The HIV virus requires the protease domain of gagpolloprotein to be cleaved before it can become infectious. This process is facilitated by the presence of gagpoll dimus which contain the protease domain and are able to detach and reattach to different locations within the lattice structure. Computer simulations have shown that the lattice structure of the immature gagpolloprotein is dynamic, even when most of the protein coat remains intact. This allows for the protease domains to detach and reattach quickly, resulting in a dimerization time of minutes or less. Additionally, the simulations suggest that the lattice structure is more stable if the interactions between the gagpoll dimus are weakened, which could explain why the virus is unable to form infectious particles until later stages of its development. This article was authored by Sikawgwa, Itsuta Saha, Savisaferian, and others.