Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

Many gene sequences in eukaryotic genomes encode entire proteins or large segments of
proteins that lack a well-structured three-dimensional fold. Disordered regions can be highly …

RNA-binding proteins (RBPs) determine RNA fate from synthesis to decay. Employing two
complementary protocols for covalent UV crosslinking of RBPs to RNA, we describe a …

Tightly packed complexes of nucleocapsid protein and genomic RNA form the core of
viruses and assemble within viral factories, dynamic compartments formed within the host …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

The intracellular environment represents an extremely crowded milieu, with a limited amount
of free water and an almost complete lack of unoccupied space. Obviously, slightly salted …