Binding of thermalized and active membrane curvature-inducing proteins

Abstract

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

arXiv comment14 pages, 15 figures

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Cited by in corpus (9)

• Reaction-Diffusion Waves Coupled with Membrane Curvature
• Perspective: New directions in dynamical density functional theory
• Vesicle budding induced by binding of curvature-inducing proteins
• Binding of Curvature-Inducing Proteins onto Biomembranes
• Binding of curvature-inducing proteins onto tethered vesicles
• Excitable reaction-diffusion waves of curvature-inducing proteins on deformable membrane tubes
• Membrane domain formation induced by binding/unbinding of curvature-inducing molecules onto both membrane surfaces
• Universal properties of active membranes
• Long-range interactions between membrane inclusions: Electric field induced giant amplification of the pairwise potential