The surface properties of c-Fos, a regulator of normal and pathologic cell growth and a modulator of phospholipid metabolism, suggest that it has the potential to transduce information through molecular reorganization, placing the. c nature of its interaction with phospholipids at the basis of its possible effects at the membrane level. Previous studies established that c-Fos induces condensation and depolarization of PIP2 films and expansion and hyperpolarization of PC. We have now explored more in depth the thermodynamic aspects of these lipid-protein interactions, finding that the Mixtures have associated hysteresis. The analysis of the excess thermodynamic functions provides evidence of entropic-enthalpic compensations that result in a favorable enthalpic contribution derived from the interaction of c-Fos with PIP2, which exceeds the unfavorable configurational entropy. On the contrary, favorable entropy terms dominate the interaction of c-Fos with PC over the unfavorable enthalpy. The free energy of hysteresis is stored as excess free energy. A shift in molecular packing-dependent surface reorganization, compared to that of ideally mixed films. indicates a gain in information content at the lipid-protein interface in mixed films of c-Fos with PIP2 but not with PC. It is postulated that the free energy stored in these mixtures could act as a bidirectional structural information transducer for dynamic compression-expansion processes occurring on the membrane surface.