Dipolar response of hydrated proteins

TL;DR

This study develops an analytical and numerical framework to understand how hydrated proteins respond to electric fields, revealing diverse dipolar behaviors influenced by protein charge and hydration, with implications for dielectric properties and protein interactions.

Contribution

The paper introduces a combined analytical and numerical approach to characterize the dipolar response of hydrated proteins, highlighting the role of hydration shells and surface charge distribution.

Findings

Ubiquitin exhibits negative dipolar susceptibility and dielectrophoresis.

Charged proteins show positive dipolar response and dielectrophoresis.

Protein-water dipolar cross-correlations extend about 2 nm from the surface.

Abstract

The paper presents an analytical theory and numerical simulations of the dipolar response of hydrated proteins. The effective dielectric constant of the solvated protein, representing the average dipole moment induced at the protein by a uniform external field, shows a remarkable variation among the proteins studied by numerical simulations. It changes from 0.5 for ubiquitin to 640 for cytochrome c. The former value implies a negative dipolar susceptibility of ubiquitin, that is a dia-electric dipolar response and negative dielectrophoresis. It means that a protein carrying an average dipole of ~240 D is expected to repel from the region of a stronger electric field. This outcome is the result of a negative cross-correlation between the protein and water dipoles, compensating for the positive variance of the protein dipole in the overall dipolar susceptibility. This phenomenon can be characterized as overscreening of protein's dipole by the hydration shell. In contrast to the neutral ubiquitin, charged proteins studied here show para-electric dipolar response and positive dielectrophoresis. The protein-water dipolar cross-correlations are long-ranged, extending approximately 2 nm from the protein surface into the bulk. The analysis of numerical simulations suggests that the polarization of the protein-water interface is strongly affected by the distribution of the protein surface charge. This component of the protein dipolar response gains in importance for high frequencies, above the protein Debye peak, when the response of the protein dipole becomes dynamically arrested. The interface response found in simulations suggests a possibility of a positive increment of the high-frequency dielectric constant of the solution compared to the dielectric constant of the solvent, in support of the observed THz absorbance of protein solutions.