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

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

Intrinsically disordered proteins and protein regions (IDPs/IDRs) exist without a single well-
defined conformation. They carry out important biological functions with multifaceted roles …

In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a
protein is determined by its amino acid sequence. This work laid the foundation for the …

The coronavirus nucleocapsid (N) is a structural protein that forms complexes with genomic
RNA, interacts with the viral membrane protein during virion assembly and plays a critical …

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 …

Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)
are functional proteins and domains that devoid stable secondary and/or tertiary structure …

Four major receptor families enable cells to respond to chemical and physical signals from
their proximal environment. The ligand-and voltage-gated ion channels, G-protein-coupled …

The eukaryotic cell is a bustling collection of macromolecules acting cooperatively to
mediate the functions required for cell viability. Specific, context-dependent and tightly …

Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …