Intrinsically disordered proteins and protein regions (IDRs) are abundant in eukaryotic
proteomes and play a wide variety of essential roles. Instead of folding into a stable …

Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical
reactions are executed inside of biomolecular condensates formed by ultradynamic …

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 …

Molecular communication in biology is mediated by protein interactions. According to the
current paradigm, the specificity and affinity required for these interactions are encoded in …

Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which
makes their structural characterization challenging. Although challenging, characterization …

Many proteins contain large structurally disordered regions or are entirely disordered under
physiological conditions. The functions of these intrinsically disordered proteins (IDPs) often …

Highly charged intrinsically disordered proteins can form complexes with very high affinity in
which both binding partners fully retain their disorder and dynamics, exemplified by the …

Fluorescence resonance energy transfer (FRET) is a powerful spectroscopic method for
measuring distances in the 2–8 nm range. Often, conformational changes and molecular …

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

Single-molecule spectroscopy is a powerful method for studying the physics of molecular
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …