Soft Matter and Complex Systems Seminar

Intrinsically disordered proteins (IDPs) are a class of biomolecules whose conformational flexibility is essential for key biological processes. Highly charged polyanionic proteins, in particular, are responsible for the regulation of biomineralisation by living organisms. We have proposed a physical framework that links the hydrodynamic and electrostatic properties of intrinsically disordered, acid-rich proteins with their function in biomineralisation, whereby the sequence-encoded charge distribution determines the hydrodynamic dimensions and flexibility of the protein chain, the local binding affinity regulates condensation behaviour, and liquid condensates that form in crowded conditions provide microenvironments that control mineral nucleation, growth, and edge development. This cascade—from protein structural disorder, through hydrodynamic behaviour and electrostatic collapse, to the formation of phase-separated liquid precursors of solid phases—represents a universal mechanism by which soft, dynamic biomolecular systems can control the formation of solid-state materials.