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2) The fact that IIPs including membrane proteins are all soluble in unsalted water, but get aggregated upon being exposed to ions, logically suggests that ions existing in the background play a central role in mediating protein aggregation, thus acting as 'dark mediators'.
Mutagenesis studies suggest that Phe residues in this region are critical in mediating protein aggregation.
These results together constitute a fact that logically suggests that despite existing in the background, salt ions play at least an equal important role in mediating protein aggregation.
Thirdly, the fact that insoluble proteins including integral membrane proteins could all be solubilized in unsalted water, but become aggregated upon being exposed to salt ions logically suggests that salt ions play central roles in mediating protein aggregation, and are thus designated as 'dark mediators' here.
This logically suggests that salt ions play a role at least as important as proteins in mediating protein aggregation.
Therefore, in aqueous environments, factors mediating protein aggregation are composed of two key categories, one associated with proteins and another with the salt ions existing in solution.
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The uncoupling mediated by T7 RNAP may in turn mediate protein aggregation.
HSP70 acts as a molecular chaperone, playing an essential role in mediating protein folding, assembly, transport, and degradation, helping to prevent protein denaturation and aggregation, and assisting in the refolding or removal of damaged proteins [ 37, 38].
Previous studies have shown that electrostatic interactions play a crucial role in mediating the process of protein aggregation (Chi, et al., 2003; Yan, et al., 2006).
We then systematically assess the role of the histidine residues in Aβ and how they mediate distinct metal-mediated, oxidative and protein aggregation stresses.
This oligomerisation model does not take into account protein aggregation mediated by the predicted β-strand at the SAS-5 C-terminus.
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