Intrinsic stiffness and <i>Θ</i>-solvent regime in intrinsically disordered proteins: Implications for liquid-liquid phase separation.

ABSTRACT: Liquid-liquid phase separation (LLPS) exhibited by intrinsically disordered proteins (IDPs) depends on the solvation state around the Θ-regime, which separates good from poor solvent. Experimentally, the Θ-solvent regime of the finite length (N) IDPs, as probed by small angle X-ray scattering (SAXS) and single molecular fluorescence resonance energy transfer (smFRET), is in disagreement. Using computer simulations of a coarse-grained IDP model, we address the effect of chain length on the Θ-regime of IDPs with polar side chains (polyglutamine) and hydrophobic side chains (polyleucine) subject to varying concentrations of cosolvents [C] , urea (denaturant) or trimethylamine N-oxide (protective osmolyte) in water. Due to their intrinsic stiffness, these IDPs are a

SUBMITTER: Baidya L 

PROVIDER: S-EPMC11840863 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature