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The goal of our project is to find patterns in the shift in the equilibrium of biochemical reactions for the ABeta receptors of amyloids, which form various structures, a change in the affinity of the receptors when they bind to various forms of amyloid structures, including both single amyloid peptides, as well as mutant peptides, as well as oligomers. We assume that the binding of receptors to different variants of amyloids will lead to a violation of the affinity when binding to their ligands, which in turn will cause changes in biochemistry at the level of the cellular response and at the level of the whole organism.
Amyloids are aggregates of proteins characterised by a fibrillar morphology
Values for stability indicator lg(cond(W))a) that were obtained by considering the interaction of wild form wtAB and interaction of mutant peptide forms mutAB from Table 1, расчетные данные величины lg(cond(W))
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