Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions.

ABSTRACT: Solutions of the intrinsically disordered, low-complexity domain of the FUS protein (FUS-LC) undergo liquid-liquid phase separation (LLPS) below temperatures T_LLPS in the 20-40° C range. To investigate whether local conformational distributions are detectably different in the homogeneous and phase-separated states of FUS-LC, we performed solid state nuclear magnetic resonance (ssNMR) measurements on solutions that were frozen on sub-millisecond time scales after equilibration at temperatures well above (50° C) or well below (4° C) T_LLPS. Measurements were performed at 25 K with signal enhancements from dynamic nuclear polarization. Crosspeak patterns in two-dimensional (2D) ssNMR spectra of rapidly frozen solutions in which FUS-LC was uniformly ¹⁵N,^13<

SUBMITTER: Wilson CB 

PROVIDER: S-EPMC11451737 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature