Protein and Water Dielectric Response in Confinement
Abstract
Molecular dynamics simulations are employed to compare the dynamics of the protein in solution, powder and in confinement between two planar slabs mimicking uncharged gold electrodes. The question addressed here is how powder and solution confinement alter the internal dynamics of the protein. We observe a major slowing down of both protein rotations and of internal shape fluctuations both in powders and in water confinement. Changes in protein dynamics are reported in terms of static and dynamic correlation function of the protein and hydration water relevant to measurements done with dielectric spectroscopy. The static dipolar susceptibilities of the protein in confinement become highly anisotropic, caused by anisotropy of the protein-water cross correlations. Anisotropy of protein’s dipolar response, already present in solution, is enhanced in confinement by anisotropy of water’s response.
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BibTeX
@misc{sarhangi2026protein,
title = {{Protein and Water Dielectric Response in Confinement}},
author = {Setare Mostajabi Sarhangi and Hari Gauli and Dmitry V. Matyushov},
howpublished = {ChemRxiv},
year = {2026},
month = sep,
doi = {10.26434/chemrxiv.15008232/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008232/v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Protein and Water Dielectric Response in Confinement
AU - Setare Mostajabi Sarhangi
AU - Hari Gauli
AU - Dmitry V. Matyushov
PY - 2026
DA - 2026/09/03
PB - ChemRxiv
DO - 10.26434/chemrxiv.15008232/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008232/v1
AB - Molecular dynamics simulations are employed to compare the dynamics of the protein in solution, powder and in confinement between two planar slabs mimicking uncharged gold electrodes. The question addressed here is how powder and solution confinement alter the internal dynamics of the protein. We observe a major slowing down of both protein rotations and of internal shape fluctuations both in powders and in water confinement. Changes in protein dynamics are reported in terms of static and dynamic correlation function of the protein and hydration water relevant to measurements done with dielectric spectroscopy. The static dipolar susceptibilities of the protein in confinement become highly anisotropic, caused by anisotropy of the protein-water cross correlations. Anisotropy of protein’s dipolar response, already present in solution, is enhanced in confinement by anisotropy of water’s response.
ER -