Abstract
A hypothesis is proposed on a potential role of protein dielectricity as an unfolding factor in protein-protein interactions. It is suggested that large protein complexes and aggregation seeds can unfold target proteins by virtue of their effect on the dielectric properties of water at the protein-solvent interface. Here, similar to the effect of membrane surfaces, protein surface can cause decrease in the local dielectric constant of solvent and thereby induce structural changes in a target protein approaching this surface. Some potential implementations of this hypothetical mechanism are also discussed.
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