Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

The protein folding problem was first articulated as question of how order arose from
disorder in proteins: How did the various native structures of proteins arise from interatomic …

Components of transcriptional machinery are selectively partitioned into specific
condensates, often mediated by protein disorder, yet we know little about how this specificity …

A number of intrinsically disordered proteins have been shown to self-assemble via liquid–
liquid phase separation into protein-rich and dilute phases. The resulting coacervates can …

The most commonly occurring intrinsically disordered proteins (IDPs) are polyampholytes,
which are defined by the duality of low net charge per residue and high fractions of charged …

Eukaryotic transcription factors (TFs) are the final integrators of a complex molecular
feedback mechanism that interfaces with the genome, consolidating information for …

Biomolecular condensates constitute a newly recognized form of spatial organization in
living cells. Although many condensates are believed to form as a result of phase …

Sequence-ensemble relationships of intrinsically disordered proteins (IDPs) are governed
by binary patterns such as the linear clustering or mixing of specific residues or residue …

Liquid–liquid phase separation (LLPS) is widely utilized by the cell to organize and regulate
various biochemical processes. Although the LLPS of proteins is known to occur in a …

Interaction strength and localization are critical parameters controlling the single-chain and
condensed-state properties of intrinsically disordered proteins (IDPs). Here, we decipher …