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The control of biofilm formation is a challenging goal that has not been reached yet in many aspects. One is the role of van der Waals forces and another the importance of mutual interactions between the adsorbing and the adsorbed biomolecules (critical crowding). Here, a combined exeperimental and theoretical approach is presented that fundamentally probes both aspects. On three model proteins, lysozyme, {alpha}-amylase and bovine serum albumin (BSA), the adsorption kinetics is studied. Composite substrates are used enabling a separation of the short- and the long-range forces. Though usually neglected, experimental evidence is given for the influence of van der Waals forces on the protein adsorption as revealed by in situ ellipsometry. The three proteins were chosen for their different conformational stability in order to investigate the influence of conformational changes on the adsorption kinetics. Monte Carlo simulations are used to develop a model for these experimental results by assuming an internal degree of freedom to represent conformational changes. The simulations also provide data on the distribution of adsorption sites. By in situ atomic force microscopy we can also test this distribution experimentally which opens the possibility to e.g. investigate the interactions between adsorbed proteins.
While a significant body of investigations have been focused on the process of protein self-assembly, much less is understood about the reverse process of a filament breaking due to thermal motion into smaller fragments, or depolymerization of subuni
We present a large-scale numerical study, supplemented by experimental observations, of a quasi-two-dimensional active system of polar rods and spherical beads confined between two horizontal plates and energised by vertical vibration. For low rod co
Surface freezing is a phenomenon in which crystallization is enhanced at a vapor-liquid interface. In some systems, such as $n$-alkanes, this enhancement is dramatic, and results in the formation of a crystalline layer at the free interface even at t
Bacterial biofilms, surface-attached communities of cells, are in some respects similar to colloidal solids; both are densely packed with non-zero yield stresses. However, unlike non-living materials, bacteria reproduce and die, breaking mechanical e
Water plays a fundamental role in protein stability. However, the effect of the properties of water on the behaviour of proteins is only partially understood. Several theories have been proposed to give insight into the mechanisms of cold and pressur