The importance of biomolecular dynamics in biocondensates was recently highlighted in the notable work of Galvanetto et al., who investigated the link between the microscopic dynamics of condensates and their mesoscopic properties by combining single-molecule fluorescence spectroscopy with all-atom MD simulations of complex coacervates of two highly charged human disordered proteins, prothymosin-α (ProTα, structural net charge -44) and histone H1 (structural net charge +53) . They showed that, although the macroscopic viscosity of the droplets is ca. 300 fold greater than that of bulk water, the dis-ordered proteins remain their highly dynamic character at the molecular scale, with polypeptide chain reconfiguration times in the nanosecond to submicrosecond regime. All-atom simulations of 96 ProTα and 80 H1 molecules in a large simulation box with ca. 4 million atoms showed that this apparent discrepancy can be explained by rapid nanosecond timescale contact exchange dynamics between charged groups, which are present at a very high local concentration in the condensate . The picture that the IDPs retain their highly dynamic character in the condensates is also underlined by recent atomistic MD simulations of the FUS low-complexity domain, which showed how different dynamic modes of the IDP are affected to different extents in the dense condensate environment .