Molecules in the condensed phase of biological condensates convert between transiently confined states and mobile states by forming dynamic percolated networks.

A colloid fractal cluster model provides a quantitative link between the atomistic features of an intrinsically disordered polypeptide and the spatial organization of the biomolecular condensate it forms.

Thermodynamic, kinetic, and dynamic analyses as well as solubility proteome profiling reveal that influenza A virus liquid inclusions may be selectively hardened with promising antiviral activity.

The condensates of activator Met4 are associated with 3D clustering of the MET regulon and its enhanced expression.

Quantitative time-resolved crosslinking mass spectrometry is developed to monitor protein interactions and dynamics inside molecular condensates and used to identify misfolding of the RNA-binding domain of FUS as a key driver of condensate-aging.

Binding of a multivalent RNA-binding protein to mRNAs that are able to form pervasive RNA–RNA interactions induces formation of mesh-like condensates, whereas binding of mostly structured mRNAs induces sphere-like condensates.

Charge complementarity between RNA and proteins may be a universal principle for phase separation in biology without requiring disorder or specific multivalent interactions.

Heterochromatin proteins compartmentalize DNA into compact structures resistant to mechanical disruption but susceptible to competitive dissolution.

Dynamical properties of liquid condensates can be quantitatively assessed by combining phase separation theory and photobleaching, which opens new avenues to understand their physicochemical properties and functioning.

The combination of optical diffraction tomography and Brillouin microscopy in a single setup enables to quantitatively map the viscoelastic properties of cellular compartments such as aggregates and stress granules in vivo.