Abstract
As demonstrated in Chaps. 1 and 3, soluble proteins retain structural integrity by shielding their backbone hydrogen bonds from competing hydration of the paired polar moieties (amide and carbonyl). Thus, a dehydron constitutes a structural deficiency since it is prone to disruptive hydration. In this chapter we describe the physical and functional properties of dehydron-rich proteins with high dehydron density. We show that dehydron clusters represent structural singularities belonging to an order-disorder twilight zone that generates a sharp local quenching of the dielectric permittivity of the surrounding medium. The functional roles of these singularities are assessed for natural proteins. Special emphasis is placed on the molecular etiology of aberrant amyloidogenic aggregation arising in dehydron-rich soluble proteins with large deviations from the golden rule of molecular architecture established in Chap. 1. Our analysis of unstable aqueous interfaces requires a description of biological water that cannot be captured by conventional continuous models, where solvent degrees of freedom are averaged out.
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Fernández, A. (2016). Dehydron-Rich Proteins in the Order-Disorder Twilight Zone. In: Physics at the Biomolecular Interface. Soft and Biological Matter. Springer, Cham. https://doi.org/10.1007/978-3-319-30852-4_5
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DOI: https://doi.org/10.1007/978-3-319-30852-4_5
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