Figure 6
From: Molecular principles of recruitment and dynamics of guest proteins in liquid droplets
Molecular dynamic (MD) simulations demonstrate different diffusion properties for folded proteins and intrinsically disordered proteins (IDPs) within p53 tetramer condensate. (A) Diffusion coefficient plots of guest proteins (Fis and p53) within p53 condensate as a function of the intermolecular energy of these guest proteins with the neighboring p53 tetramers. The inset shows the distribution of the calculated D values for Fis and p53. (B) Similar plot as in panel (A) for four folded proteins (blue) and two IDPs (red). The errors denote the standard deviation reflecting the heterogeneity in the energy and D value. (C) Projections of three independent trajectories (in reddish or bluish colors) of diffusion for two folded guest proteins (Fis and GFP) and two IDPs (p53 and poly-R) within p53 condensate, illustrating greater restricted diffusion of the IDPs compared with the folded proteins (left panels). Gray lines represent the location of the center of mass of the 20 tetrameric p53 that comprise its liquid-like condensate during the simulations. Snapshot of the guest proteins in p53 condensate illustrate the extensive interactions of the IDPs with p53 via intermolecular interactions between their disordered regions (right panels). The folded proteins can be trapped in voids and interact less tightly with the p53 condensate. The host p53 tetramer are shown in green, with the core and Tet domains as large spheres. The guest folded proteins and IDP are shown in blue and red, respectively. For the guest p53, the core and Tet domains, respectively, are shown in yellow and orange, and the N- and C-terminal disordered domains and linker are shown in red, purple, and pink, respectively.
