Binding of thermalized and active membrane curvature-inducing proteins

Membrane phase behavior induced by the binding of curvature-inducing proteins is studied a combination analytical and numerical approaches. In thermal equilibrium under detailed balance between unbinding, membrane exhibits three phases: an unbound uniform flat (U), bound (B), separated/corrugated (SC). SC phase, form hexagonally-ordered bowl-shaped domains. The transitions U phases B are second order first order, respectively. At small spontaneous curvature protein or high surface tension, transition becomes continuous. Moreover, first-order found at zero driven Casimir-like interactions rigid proteins. Furthermore, nonequilibrium dynamics investigated addition active unbinding constant rate. processes alter stability phase.