Structural biology plays a pivotal role in understanding complex molecular assemblies that
encode vital functions in cellular processes. The determination of the nucleic acids, protein …

Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late
1990s when a few groups, working independently, convinced the community that these …

The emergence of intrinsically disordered proteins (IDPs) has challenged the classical
protein structure-function paradigm by introducing a new paradigm of “coupled binding and …

In this thematic minireview series, the JBC presents six exciting articles on low complexity or
intrinsically disordered proteins (IDPs). The dynamical and fluctuating structures of IDPs or …

Intrinsically disordered proteins (IDPs) are an important class of functional proteins that is
highly prevalent in biology and has broad association with human diseases. In contrast to …

Proteins may vary from being rigid to having flexible regions to being completely disordered,
either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered …

Intrinsically disordered proteins (IDPs) lack a persistent defined structure in the absence of
biomolecular interactions. In the early days of the protein structure-function paradigm …

The classical view holds that proteins fold into essentially unique three-dimensional
structures before becoming biologically active. However, studies over the last several years …

Intrinsically disordered proteins (IDPs) challenge current views on biomolecular
communication because these proteins participate in functional biological complexes …

Abstract Disordered Proteins (IDPs) challenge the conventional structure-function paradigm
by exhibiting a lack of tertiary structure while performing a diverse array of functions. This …