The N-terminal repressor domain of neural restrictive silencer factor (NRSF) is an
intrinsically disordered protein (IDP) that binds to the paired amphipathic helix (PAH) …

Intrinsically disordered proteins (IDPs) are proteins that lack a unique three-dimensional
structure in their native state. Many have, however, been found to fold into a defined …

Intrinsically disordered proteins or regions (IDRs) differ from their well-folded counterparts by
lacking a stable tertiary state. Instead, IDRs exist in an ensemble of conformations and often …

To understand the interplay of residual structures and conformational fluctuations in the
interaction of intrinsically disordered proteins (IDPs), we first combined implicit solvent and …

Intrinsically disordered proteins (IDPs) are a class of proteins lacking a well-defined
secondary structure. Instead, they are able to attain multiple conformations, bind to multiple …

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) and intrinsically disordered regions (IDRs) of proteins
are very common and instrumental for cellular signaling. Recently, a number of studies have …

Intrinsically disordered proteins (IDPs) have no fixed three-dimensional (3D) structures
under physiological conditions, with the content being about 51% in human proteomics …

Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently
emerged as major therapeutic targets for various diseases. Unlike traditional proteins that …

Molecular simulations of intrinsically disordered proteins (IDPs) are challenging because
they require sampling a very large number of relevant conformations, corresponding to a …