Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.
CPEB4's switch from translational repressor to activator is regulated during cell cycle by hyperphosphorylation of its intrinsically disordered domain, which controls its phase-separation into RNA-containing liquid-like droplets.
The C-terminus of A2A receptor drives oligomer formation via an intricate network of disulfide bonds, hydrogen bonds, electrostatic interactions, and hydrophobic interactions, all of which are enhanced by depletion interactions.
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.
GCNA proteins comprise a previously unnoticed family of proteins that has been enriched in cells carrying a heritable genome since the invention of sexual reproduction in eukaryotes, and has had reproductive function for at least 600 million years.
DNA replication initiation proteins contain a disordered domain that impacts each stage of their function, from chromatin recruitment and initiator co-assembly to the subsequent displacement of the factors from chromatin.