It is unclear how disease mutations impact intrinsically disordered protein regions (IDRs),
which lack a stable folded structure. These mutations, while prevalent in disease, are …

Highlights•Not all IDRs undergo liquid–liquid phase separation.•IDRs are not necessary for
protein phase separation.•A stickers-and-spacers framework helps conceptualizing IDR …

Intrinsically disordered proteins (IDPs) have been implicated in a number of human
diseases, including cancer, diabetes, neurodegenerative and cardiovascular disorders …

Intrinsically disordered protein regions (IDRs)-regions that do not fold into a fixed three-
dimensional structure but instead exist in a heterogeneous ensemble of conformations-have …

The effects of disease mutations on protein structure and function have been extensively
investigated, and many predictors of the functional impact of single amino acid substitutions …

Intrinsically disordered regions (IDRs) make up ca. 30% of the proteome of most eukaryotes,
and are involved in a diverse set of functions. Conventional sequence alignment tools …

Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under
physiological conditions in vitro. They are highly abundant in nature and their functional …

Phase separation of intrinsically disordered proteins (IDPs) commonly underlies the
formation of membraneless organelles, which compartmentalize molecules intracellularly in …

The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …

Intrinsically disordered proteins (IDPs) constitute a broad set of proteins with few uniting and
many diverging properties. IDPs—and intrinsically disordered regions (IDRs) interspersed …