$\epsilon_{I,S}=2.79~\epsilon_{A,S}$ and $\epsilon_{F,S}=6.08~\epsilon_{A,S}$ by adopting the adsorption rate constants as in the theoretical model of Lu et al. [@Lu1994], that reflect the experimental observation that Fib has the strongest affinity for several surfaces and albumin the weakest.

The Numerical Method
====================

We perform MD simulations at constant $T$, constant volume $V$ and constant number of proteins $N_i$, in a parallelepiped with two square faces and four rectangular faces. A square face is occupied by the attractive surface, the other by a wall interacting with the proteins through the repulsive part of the potential in Eq.(\[1\]). We apply periodic boundary conditions (pbc) along the four rectangular faces. The volume concentrations of proteins is taken to match the average concentrations of the human plasma, with $c_{A}=4.25$ g/dl, $c_{I}=1.25$ g/dl and $c_{F}=0.325$ g/dl, at $X_P=100\%$ plasma concentration in blood. When a protein is adsorbed on (released by) the surface, we keep its bulk concentrations constant by inserting (deleting) a protein of the same family in a randomly-chosen empty (occupied) space of the box.

Experiments are usually carried out for highly diluted plasma, at concentration as small as $X_P=0.1\%$, to slow down the adsorption rate to minutes or hours, allowing precise measurements. However, such 