β Scribed by V.P. Zhdanov; B. Kasemo
No coin nor oath required. For personal study only.
Adapting a hard hexagon model to describing protein adsorption, we show by using Monte Carlo simulations that the ordering of adsorbed proteins may strongly depend on the relative location of the hydrophilic and hydrophobic patches on their surface. Specifically, proteins may form dimers, trimers, small rings, and zig-zag or straight chains or islands consisting of such fragments.
π SIMILAR VOLUMES
Recent developments in experimental and theoretical studies on competitive adsorption, thermodynamic incompatibility of mixing of proteins, and phase separation in mixed proteins films at interfaces are reviewed. A critical analysis of these data indicates that a basic understanding of protein-water
Previous investigation implicated surface charge and surface energy as factors which affect blood clotting. The present paper attempts to explore the theoretical basis for these affects. Expressions are also derived relating change and interfacial tension to the binding constants of the protein. Fin