Hydrophobic interactions are involved in and believed to be the fundamental driving force of
many chemical and biological phenomena in aqueous environments. This review focuses …

Highlights•The accuracy of physical models used in protein-folding simulations is
assessed.•This assessment is based on data from very long molecular dynamics …

Abstract The SARS-CoV-2 nucleocapsid (N) protein is an abundant RNA-binding protein
critical for viral genome packaging, yet the molecular details that underlie this process are …

Many proteins can be partially or completely disordered under physiological conditions.
Structural characterization of these disordered states using experimental methods can be …

The functions of intrinsically disordered proteins (IDPs) are governed by relationships
between information encoded in their amino acid sequences and the ensembles of …

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

One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …

The dimensions of unfolded and intrinsically disordered proteins are highly dependent on
their amino acid composition and solution conditions, especially salt and denaturant …

An increasing number of studies using molecular dynamics (MD) simulations of unfolded
and intrinsically disordered proteins (IDPs) suggest that current force fields sample …