Intrinsically disordered proteins (IDPs) have attracted wide interest over the past decade due
to their surprising prevalence in the proteome and versatile roles in cell physiology and …

Many cellular functions, including signaling and regulation, are carried out by intrinsically
disordered proteins (IDPs) binding to their targets. Experimental and computational studies …

For more than a century, molecular and structural biology, biochemistry, and protein
biophysics have been dominated by a “rigid” or “semi-rigid” view of a functional 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 focus of the computational structural biology community has taken a dramatic shift over
the past one-and-a-half decades from the classical protein structure prediction problem to …

Intrinsically disordered proteins (IDPs) are unorthodox proteins that do not form three-
dimensional structures under non-denaturing conditions, but perform important biological …

Understanding signaling and other complex biological processes requires elucidating the
critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent∼ …

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 …

Many full-length proteins and protein regions lack stable tertiary and/or secondary structure
under physiological conditions in vitro. These proteins and regions, known as intrinsically …

We have performed a 4-μs molecular dynamics simulation to investigate the native
conformational preferences of the intrinsically disordered kinase-inducible domain (KID) of …