displacement and liberation rate constant do not depend on the incoming protein [@LeDuc1995]. They applied the model to rationalize data of a ternary solution mixture with Albumin, high molecular weight Kininogen and Fibrinogen, accounting also for the deformation of the semipermanently adsorbed proteins. As a result, LeDuc et al. found that, to fit the data, the first two proteins should occupy approximately fourfold more space in the semipermanent state while Fibrinogen would have a much smaller change.

This is at variance with what recent experiments show for rod-like proteins as the Fibrinogen. This elongated protein, although deforms less then Albumin when adsorbed on an extended surface, can undergo a large rearrangement from an initial “lying down” stage (with its long axis parallel to the surface) to a “standing up” conformation (long axis perpendicular to the surface). This conformational change results in a large difference in the occupied surface [@Roach2005].

While the models based on kinetic equations are useful to qualitatively reproduce the experimental data by fitting the rate constants, they are less instructive about the mechanisms that at molecular level control the phenomenon. To give an insight into how the competition between sizes, bulk concentrations, surface affinities, diffusion constants and 