From coarse-grained molecular dynamics simulations to continuum models of biomolecular condensation
- 1National Institute of Chemistry
Abstract
Biomolecular condensation contributes to cellular organization and the regulation of numerous biochemical processes. Capturing its dynamics on large spatio-temporal scales requires a macroscopic model that accurately describes both thermodynamic forces and molecular transport. Here, we investigate the applicability of the Cahn-Hilliard equation for modeling phase-separation dynamics in intrinsically disordered proteins. Using the low-complexity domain of FUS as a model system for biomolecular condensation, we perform coarse-grained molecular dynamics simulations to infer the free-energy functional and mobility coefficient entering the Cahn-Hilliard equation. The resulting continuum model accurately describes the growth of initial concentration fluctuations in the spinodal regime and the subsequent morphological evolution of the concentration fields during coarsening. We find that the free-energy functional is transferable across different stages of phase separation, whereas the mobility is not. During coarsening, we identify two kinetic regimes characterized by distinct mobilities, which persist even when a concentration-dependent mobility is introduced.
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BibTeX
@misc{hubman2026from,
title = {{From coarse-grained molecular dynamics simulations to continuum models of biomolecular condensation}},
author = {A. Hubman and T. Potisk and F. Merzel},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.14.759104},
url = {https://www.biorxiv.org/content/10.64898/2026.10.14.759104v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - From coarse-grained molecular dynamics simulations to continuum models of biomolecular condensation
AU - A. Hubman
AU - T. Potisk
AU - F. Merzel
PY - 2026
DA - 2026/10/14
PB - bioRxiv
DO - 10.64898/2026.10.14.759104
UR - https://www.biorxiv.org/content/10.64898/2026.10.14.759104v1
AB - Biomolecular condensation contributes to cellular organization and the regulation of numerous biochemical processes. Capturing its dynamics on large spatio-temporal scales requires a macroscopic model that accurately describes both thermodynamic forces and molecular transport. Here, we investigate the applicability of the Cahn-Hilliard equation for modeling phase-separation dynamics in intrinsically disordered proteins. Using the low-complexity domain of FUS as a model system for biomolecular condensation, we perform coarse-grained molecular dynamics simulations to infer the free-energy functional and mobility coefficient entering the Cahn-Hilliard equation. The resulting continuum model accurately describes the growth of initial concentration fluctuations in the spinodal regime and the subsequent morphological evolution of the concentration fields during coarsening. We find that the free-energy functional is transferable across different stages of phase separation, whereas the mobility is not. During coarsening, we identify two kinetic regimes characterized by distinct mobilities, which persist even when a concentration-dependent mobility is introduced.
ER -