  We have studied the adsorption kinetics of the protein amylase at
solid/liquid interfaces. Offering substrates with tailored properties, we are
able to separate the impact of short- and long-range interactions. By means of
a colloidal Monte Carlo approach including conformational changes of the
adsorbed proteins induced by density fluctuations, we develop a scenario that
is consistent with the experimentally observed three-step kinetics on specific
substrates. Our observations show that not only the surface chemistry
determines the properties of an adsorbed protein layer but also the van der
Waals contributions of a composite substrate may lead to non-negligible
effects.
