Liquid-liquid phase separation of a surfactant-solubilized membrane   protein
  The phase behavior of membrane proteins stems from a complex synergy with the amphiphilic molecules required for their solubilization. We show that ionization of a pH-sensitive surfactant, LDAO, bound to a bacterial photosynthetic protein, the Reaction Center (RC), leads in a narrow pH range to protein liquid-liquid phase separation in surprisingly stable `droplets', forerunning reversible aggregation at lower pH. Phase segregation is promoted by increasing temperature and hindered by adding salt. RC light-absorption and photoinduced electron cycle are moreover strongly affected by phase segregation. 
R. Piazza, M. Pierno, E. Vignati, G. Venturoli, F. Francia, A.   Mallardi, and G. Palazzo