Composition variation and underdamped mechanics near membrane proteins and coats

Abstract

We study the effect of membrane proteins on the shape, composition and thermodynamic stability of the surrounding membrane. When the coupling between membrane composition and curvature is strong enough the nearby composition and shape both undergo a transition from over-damped to under-damped spatial variation, well before the membrane becomes unstable in the bulk. This transition is associated with a change in the sign of the thermodynamic energy and hence has the unusual features that it can favour the early stages of coat assembly necessary for vesiculation (budding), while suppressing the activity of mechanosensitive membrane channels and transporters. Our results also suggest an approach to obtain physical parameters that are otherwise difficult to measure.