Hypothesis: The unfolding power of protein dielectricity

Intrinsically Disordered Proteins
Vladimir N Uversky

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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Citations

Jan 1, 2013·Intrinsically Disordered Proteins·Leonid Breydo

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Methods Mentioned

BETA
NMR
X-ray
protein folding

Software Mentioned

VMD

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