Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

Intrinsically disordered proteins (IDPs) are often modeled using ideas from polymer physics
that suggest they smoothly explore all corners of configuration space. Experimental …

Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which
makes their structural characterization challenging. Although challenging, characterization …

Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structures, thus
challenging the archetypal notion of structure–function relationships. Determining the …

Water radical cations, the crucial intermediates in many aqueous reactions and biochemical
processes, are difficult to investigate experimentally due to their short lifetime and low …

Experimental studies on intrinsically disordered and unfolded proteins have shown that in
isolation they typically have low populations of secondary structure and exhibit distance …

Proteins are marginally stable molecules that fluctuate between folded and unfolded states.
Here, we provide a high-resolution description of unfolded states under refolding conditions …

The dimensions that unfolded proteins, including intrinsically disordered proteins (IDPs),
adopt in the absence of denaturant remain controversial. We developed an analysis …

An accurate account of disordered protein conformations is of central importance to
deciphering the physicochemical basis of biological functions of intrinsically disordered …

Over the last two decades, intrinsically disordered proteins and protein regions (IDRs) have
emerged from a niche corner of biophysics to be recognized as essential drivers of cellular …