Abstract
The high concentration of proteins and other biological macromolecules inside biomolecular condensates leads to dense and confined environments, which can affect the dynamic ensembles and the time-scales of the conformational transitions. Here we use atomistic molecular dynamics (MD) simulations of the intrinsically disordered low complexity domain (LCD) of the human fused in sarcoma (FUS) RNA-binding protein to study how self-crowding inside a condensate affects the dynamic motions of the protein. We found a heterogeneous retardation of the protein dynamics in the condensate with respect to the dilute phase, with large-amplitude motions being strongly slowed by up to two orders of magnitude, whereas small-scale motions, such as local backbone fluctuations and side-chain rotations, are less affected. The results support the notion of a liquid-like character of the condensates and show that different protein motions respond differently to the environment.
Competing Interest Statement
The authors have declared no competing interest.
Footnotes
1. Error bars have been added to Fig. 2 and Fig. 3 2. Fig. 4B is now represented in semi-log scale 3. The introduction and conclusion have been modified 4. Extra figure added to supplemental section (Fig. S2) 5. New references have been aded
