Abstract
The aggregation of proteins in membranes accompanied by a higher elasticity of the membrane in the vicinity of the proteins and a shift of the crystalline–liquid crystalline phase transition to higher temperatures is shown to be caused by an indirect interaction between the ’’annuli’’ of proteins. In the neighborhood of proteins the order‐parameter fluctuations will be decreased, building a region of relative stability, which lowers the free energy of the system. On the base of a linear response approximation an effective potential is defined and an explicit expression for the distance‐dependent interaction of two cylindrical model proteins is derived.