Highlights•Improvements in all-atom simulations and implicit solvent models now allow IDP
simulations with realistic dimensions to be performed.•Native-centric coarse-grained …

The sustenance of life depends on the high degree of organization that prevails through
different levels of living organisms, from subcellular structures such as biomolecular …

Some frequently encountered deficiencies in all-atom molecular simulations, such as
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …

There has been a long-standing controversy regarding the effect of chemical denaturants on
the dimensions of unfolded and intrinsically disordered proteins: A wide range of …

Chemical denaturants are the most commonly used agents for unfolding proteins and are
thought to act by better solvating the unfolded state. Improved solvation is expected to lead …

The traditional structure–function paradigm has provided significant insights for well-folded
proteins in which structures can be easily and rapidly revealed by X-ray crystallography …

Intrinsically disordered proteins (IDPs) are now widely recognized as playing critical roles in
a broad range of cellular functions as well as being implicated in diverse diseases. Their …

Förster resonance energy transfer (FRET) is a powerful tool for elucidating both structural
and dynamic properties of unfolded or disordered biomolecules, especially in single …

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

We use all-atom molecular simulation with explicit solvent to study the properties of selected
intrinsically disordered proteins and unfolded states of foldable proteins, which include …