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It is known that the molecular crowding effect on protein aggregation is non-linear and that as the protein concentration increases, the aggregation increases exponentially [38].
Wang et al. [ 6] proposed that "molecular crowding" effect and evolution of linker sequences can explain differences between length of orthologous sequences in super-kingdoms.
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Here, we review the accumulated evidence that the nm-scaled dimensions and conformational changes of these proteins support functions of the complement system with regard to tissue distribution, molecular crowding effects, avidity binding, and conformational regulation of complement activation.
Therefore, molecular crowding effects are not simulated.
In contrast, GridCell implicitly exhibits molecular crowding effects by allowing inter-particle collisions.
The simulations are performed within a virtual cytoskeleton enriched with further crowding elements, which allows the analysis of molecular crowding effects on intracellular diffusion and reaction rates.
Experimental data already existing for both polyelectrolyte and molecular crowding effects strongly suggests a very high impact on the cytoskeletal behavior.
So far, molecular crowding effects are neither considered in most theoretical models nor are they deliberately included in reconstituted experimental systems.
This result is consistent with a previous report that even GFP molecules diffuse much slower in HCs possibly due to molecular crowding effects (Bancaud et al., 2009).
Moreover, the (moderate) increase in reactant concentration might be counteracted by molecular crowding effects and increases in viscosity (Miermont et al., 2013).
In good agreement with this observation, a previous report demonstrated via Fluorescence Correlation Spectroscopy (FCS) measurements that even GFP molecules diffuse much slower in heterochromatic regions possibly due to molecular crowding effects (Bancaud et al., 2009).
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