The ever increasing computer power, together with the improved accuracy of atomistic force
fields, enables researchers to investigate biological systems at the molecular level with …

There is mounting evidence that Alzheimer's disease progression and severity are linked to
neuronal membrane damage caused by aggregates of the amyloid-β (A β) peptide …

The common conception of intrinsically disordered proteins (IDPs) is that they stochastically
sample all possible configurations driven by thermal fluctuations. This is certainly true for …

It is now increasingly evident that a large fraction of the human proteome comprises proteins
that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have …

Intrinsically disordered proteins (IDPs) lack a rigid three-dimensional structure and populate
a polymorphic ensemble of conformations. Because of the lack of a reference conformation …

Phenotypic plasticity is the ability of individual genotypes to produce different phenotypes in
response to environmental perturbations. We previously postulated how conformational …

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 protein p27, a prominent regulatory protein in eukaryotes and an intrinsically disordered
protein (IDP), regulates cell division by causing cell cycle arrest when bound in ternary …

The rationale for replacing the old binary of structure–function with the trinity of structure,
disorder, and function has gained considerable ground in recent years. A continuum model …

Intrinsically disordered proteins (IDPs) lack a well-defined three-dimensional structure but
do exhibit some dynamical and structural ordering. The structural plasticity of IDPs indicates …