Single-molecule FRET (smFRET) has become a mainstream technique for studying
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …

Intrinsically disordered proteins (IDPs) play important roles in cellular functions. The inherent
structural heterogeneity of IDPs makes the high-resolution experimental characterization of …

The first genuine high-resolution single particle cryo-electron microscopy structure of a
membrane protein determined was a transient receptor potential (TRP) ion channel, TRPV1 …

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 …

An increasing number of protein interaction domains and their targets are being found to be
intrinsically disordered proteins (IDPs). The corresponding target recognition mechanisms …

Highlights•Multivalent interactions of intrinsically disordered proteins (IDP) are highly
dynamic, leading to complex binding thermodynamics and kinetics and various functional …

The molecular dynamics (MD) method is a promising approach toward elucidating the
molecular mechanisms of intrinsically disordered regions (IDRs) of proteins and their fuzzy …

Biomolecular condensation is involved in various cellular processes; therefore, regulation of
condensation is crucial to prevent deleterious protein aggregation and maintain a stable …

The intrinsically disordered C-terminal domain (CTD) of protein 4.1 G is able to specifically
bind a 26-residue intrinsically disordered region of NuMA, forming a dynamic fuzzy complex …

Intrinsically disordered proteins or hybrid proteins with ordered domains and disordered
regions (both collectively designated as IDP (R) s) defy the well-established structure …