The development of molecular descriptions of intrinsically disordered proteins (IDPs) is
essential for elucidating conformational transitions that characterize common …

Intrinsically disordered proteins (IDPs) represent a new frontier in structural biology since the
primary characteristic of IDPs is that structures need to be characterized as diverse …

Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of the
human genome, and the development of meaningful molecular descriptions of these …

Intrinsically disordered proteins (IDPs) are increasingly recognized for their important roles
in a range of biological contexts, both in normal physiological function and in a variety of …

Intrinsically disordered proteins (IDPs) are not well described by a single 3D conformation
but by an ensemble of them, which makes their structural characterization especially …

In order to understand the conformational behavior of intrinsically disordered proteins (IDPs)
and their biological interaction networks, the detection of residual structure and long-range …

Intrinsically disordered proteins (IDPs) play fundamental roles in signaling, regulation, and
cell homeostasis by specifically interacting with their partners. The structural characterization …

Combining structural proteomics experimental data with computational methods is a
powerful tool for protein structure prediction. Here, we apply a recently-developed approach …

Intrinsically disordered proteins (IDPs) are abundant in eukaryotic proteomes, play a major
role in cell signaling, and are associated with human diseases. To understand IDP function it …

The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …