for (a) Fib, (b) IgG and (c) Alb, at $X_P=100\%$ ($\Delta$), $X_P=50\%$ (), and $X_P=25\%$ (). In (a) the dashed lines are guide to the eyes, showing that the linear regime is more extended than at $T=300$ K. For Alb the $C^S_A$ of saturation is non-monotonic with $X_P$. []{data-label="fdil120"}](Fig5)

By comparing the $C_i^S$ at different $X_P$ for the same protein (Fig. \[fdil120\]), we find that second step in the Fib adsorption is now more extended in time. This result is consistent with what has been observed in the experiments from single protein absorption when conformational changes occur [@Bellion2008]. Moreover, our analysis for competitive adsorption shows, as for $T=300$ K, that the linear regime of Fib adsorption coincides with the end of the desorption of the Alb and the beginning of desorption of IgG. However, at $T=120$ K, the ability of Fib to displace IgG is much more limited than at $T=300$ K, because the displacement requires too much energy. This fact, on one hand, limits the adsorption of Fib, on the other hand does not allows Alb to re-adsorb. Nevertheless, the competition between Fib and IgG is enough to stop the desorption of Alb that now saturates at a value 