A central challenge in the study of intrinsically disordered proteins is the characterization of
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …

Biological functions of intrinsically disordered proteins (IDPs), and proteins containing
intrinsically disordered regions (IDRs) are often mediated by short linear motifs, like proline …

In contrast to the “lock-and-key” model underlying the long-term success of structural biology
and rational drug design, intrinsically disordered proteins (IDPs) exist in an ensemble of …

Many proteins recognise other proteins via mechanisms that involve the folding of
intrinsically disordered regions upon complex formation. Here we investigate how the …

Intrinsically disordered regions (IDRs) are critical for cellular function, yet often appear to
lack sequence conservation when assessed by multiple sequence alignments. This raises …

Intrinsically disordered regions (IDRs) are critical for cellular function yet often appear to lack
sequence conservation when assessed by multiple sequence alignments. This raises the …

Intrinsically disordered proteins (IDPs), which in isolation do not adopt a well-defined tertiary
structure but instead populate a structurally heterogeneous ensemble of interconverting …

Intrinsically disordered proteins (IDPs) or regions (IDRs) exhibit biological activities and play
important roles in cell signaling and regulation, yet they do not form a well-defined three …

Intrinsically disordered proteins (IDPs) populate a range of conformations that are best
described by a heterogeneous ensemble. Grouping an IDP ensemble into “structurally …

In recent years, protein science has been revolutionized by the discovery of intrinsically
disordered proteins (IDPs). In contrast to the classical paradigm that a given protein …