Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, U.K.
Department of Physics and Astronomy, Institute for the Physics of Living Systems, University College London, London, WC1E 6BT, U.K.
J Phys Chem Lett. 2022 Aug 25;13(33):7853-7860. doi: 10.1021/acs.jpclett.2c01986. Epub 2022 Aug 17.
A self-consistent analytical solution for binodal concentrations of the two-component Flory-Huggins phase separation model is derived. We show that this form extends the validity of the Ginzburg-Landau expansion away from the critical point to cover the whole phase space. Furthermore, this analytical solution reveals an exponential scaling law of the dilute phase binodal concentration as a function of the interaction strength and chain length. We demonstrate explicitly the power of this approach by fitting experimental protein liquid-liquid phase separation boundaries to determine the effective chain length and solute-solvent interaction energies. Moreover, we demonstrate that this strategy allows us to resolve differences in interaction energy contributions of individual amino acids. This analytical framework can serve as a new way to decode the protein sequence grammar for liquid-liquid phase separation.
推导出了用于二元 Flory-Huggins 相分离模型的节点浓度的自洽解析解。我们表明，这种形式将吉布斯-朗道展开的有效性从临界点扩展到覆盖整个相空间。此外，该解析解揭示了稀相节点浓度作为相互作用强度和链长函数的指数标度律。我们通过拟合实验蛋白质液-液相分离边界来明确展示了这种方法的威力，以确定有效链长和溶质-溶剂相互作用能。此外，我们证明这种策略可以使我们分辨出单个氨基酸的相互作用能贡献的差异。这个分析框架可以作为一种新的方法来解码液-液相分离的蛋白质序列语法。
