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For systems that involve proteins, which tend to interact strongly with surfaces through hydrophobic interactions, surface passivation is often required to retain the integrity of the system.
Considering the adsorbent adsorbate interactions, surface modifications also improve the selectivity of MCM-41 [16].
In addition, electrostatic interactions (surface charge) and viscoelastic properties (elastic modulus) of the substrate have been shown to influence the bacterial adherence (Brady [1999]; Rosenhahn et al. [2009]).
However, Kow only reflects hydrophobic interactions and does not accurately account for electrostatic interactions, surface complexation, hydrogen bonding, cation-exchange, or bridging that may vary significantly with changes in pH, OM, and ionic strength [1].
Our study is based on a random site-diluted classical Heisenberg Hamiltonian with nearest-neighbor interactions, surface and core anisotropies, and a Monte Carlo Metropolis approach with simulated annealing for energy minimization.
The general model of continuous media proposed in the present paper allows analysis of various particular scale effects, e.g., cohesive interactions, surface tensions, etc., both in volume and on the surface within the unified continuum description.
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Analyses of the interaction surfaces using the protein interactions, surfaces and assemblies (PISA) server 19 yielded interface areas of approximately 870 Å in both dimers.
Crucially, dimerization arises from two potentially independent interactions surfaces at the "north" and "south" poles of the torus.
If domains in each of the proteins were known to interact, these are displayed as the potential interaction surface that explains the protein-protein interaction in the HPRD.
In both classes, residues 18 20 provide a conserved interaction surface.
The interaction surface of the Rho NusG complex is unknown.
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