Table 2. Parameters for the CG Model of Proteins^a.

	HSA	Tf	Fib
Rh [nm]	2.728	3.7216	8.529
RS [nm]	3.630	3.725	11.030,31
ε [kBT]	212	212	212
M [kDa]	67	80	340
ϕ [mV]	–1532	–1033,34	–2031
AH [kBT]	9.75	8.4	7
Nmax	550	450	120

^aR_h and R_S are the two characteristic length-scales of a protein in each conformation: R_h is obtained from the maximum surface concentration of each protein, and R_S is the hydrodynamic radius. ε is the repulsion energy between two adsorbed proteins at the shorter diameter distance in eq S9 in SI. M is the mass of the protein (as specified by Sigma-Aldrich), ϕ is the zeta-potential in PBS, A_H is the Hamaker constant, calibrated as explained in the text, for the DLVO interaction potential with silica NP in eq S8 in SI. N_max is the maximum number of adsorbed molecules forming a full monolayer on the NP, as computed by simulations. We indicate the adopted units near the parameters and the used references, if applicable, near their values.