ArticleJACS Au2026
Simulating Thermoresponsive Behavior of Disordered Proteins with Temperature-Dependent Coarse-Grained Potentials Derived from Hydration Free Energies.
Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Thermoresponsive phase transitions of intrinsically disordered proteins (IDPs), including both upper critical solution temperature (UCST) and lower critical solution temperature (LCST) transitions, are widely observed in natural and synthetic sequences. However, most existing coarse-grained (CG) models employ temperature-independent interactions and fail to capture solvation-driven LCST behavior. Here, we bridge the gap between atomistic hydration and macroscopic phase separation. Leveraging 500 μs long extensive all-atom molecular dynamics simulations, we reveal a fundamental linear correlation between the temperature-dependent inter-residue interaction strengths and hydration free energies. Furthermore, we demonstrate that the heterotypic interactions at the molecular level can be well approximated by a simple combination of the homotypic interactions. We incorporate these thermodynamic insights into a physics-based framework,
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