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

The sequence–structure–function paradigm of proteins has been revolutionized by the
discovery of intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) …

Intrinsically disordered proteins (IDPs), which lack folded structure and are disordered under
nondenaturing conditions, have been shown to perform important functions in a large …

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 …

Unconstrained atomistic simulations of intrinsically disordered proteins and peptides (IDP)
remain a challenge: widely used,“general purpose” water models tend to favor overly …

Förster Resonance Energy Transfer (FRET) between two fluorescent proteins can be
exploited to create fully genetically encoded and thus subcellularly targetable sensors …

Proteins containing intrinsically disordered regions (IDRs) are ubiquitous within
biomolecular condensates, which are liquid-like compartments within cells formed through …

Abnormally expanded polyglutamine domains in proteins are associated with several
neurodegenerative diseases, of which the best known is Huntington's. Expansion of the …

Histone tails are highly flexible N-or C-terminal protrusions of histone proteins which
facilitate the compaction of DNA into dense superstructures known as chromatin. On a …

The dynamics of unfolded proteins are important both for the process of protein folding and
for the behavior of intrinsically disordered proteins. However, methods for investigating the …