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The dendrite branching receptor HPO-30 modulates actin dynamics by binding to both WAVE complex and actin filaments.

Clustering the B cell receptor generates a membrane domain analogous to the liquid-ordered phase, localizing proteins involved in early receptor activation.

Minimal changes allow an ancestral, unfolded peptide to adopt a known fold by repetition, illuminating a possible path for the emergence of folded proteins at the origin of life.

The intrinsically disordered N-terminus of Sfr1 contains two Rad51 binding sites that facilitate Rad51 filament stabilization and ATPase stimulation by the Swi5-Sfr1 complex, leading to efficient Rad51-driven strand exchange.

Molecular simulations show how hydrophobicity and conformational disorder underlie the phase separation of elastin-like peptides and the elasticity of human tissues.

Exploration of the phenotype space corresponding to the sequence space of viable SARS-CoV-2 nucleocapsid protein species reveals significant diversity of biophysical characteristics, nonlocal mutation effects, and functional constraints.

Dimers of Bak assemble into clusters without using a distinct protein-protein interface, which may explain the apparent difficulties in obtaining high resolution structures of the pore complex and in targeting dimer-dimer interactions to regulate apoptosis.

Statistics on the frequencies of pi interactions in folded protein structures enable successful prediction of intrinsically disordered protein phase separation, with clear implications for a physical understanding of cellular organization.

P granule assembly depends in part on protein-protein interactions that drive condensation independent of RNA.

An inorganic tin oxochloride cluster specifically binds to an intrinsically disordered, histidine-rich, low complexity protein region and arrests de novo transcription initiation without affecting reinitiation.