Multivalent proteins and nucleic acids, collectively referred to as multivalent associative
biomacromolecules, provide the driving forces for the formation and compositional …

Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

Prion-like low-complexity domains (PLCDs) are involved in the formation and regulation of
distinct biomolecular condensates that form via phase separation coupled to percolation …

Optimum protein function and biochemical activity critically depends on water availability
because solvent thermodynamics drive protein folding and macromolecular interactions …

Intrinsically disordered proteins and protein regions (IDRs) are abundant in eukaryotic
proteomes and play a wide variety of essential roles. Instead of folding into a stable …

The molecular machinery that enables life has evolved in water, yet many of the organisms
around us are able to survive even extreme desiccation. Especially remarkable are single …

Biomolecular condensates form via processes that combine phase separation and
reversible associations of multivalent macromolecules. Condensates can be two-or …

Macromolecular crowding affects the activity of proteins and functional macromolecular
complexes in all cells, including bacteria. Crowding, together with physicochemical …

Life emerges from thousands of biochemical processes occurring within a shared
intracellular environment. We have gained deep insights from in vitro reconstitution of …

In response to variations in osmotic stress, in particular to hypertonicity associated with
biological dysregulations, cells have developed complex mechanisms to release their …