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

A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

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

Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

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

Many nonequilibrium, active processes are observed at a coarse-grained level, where
different microscopic configurations are projected onto the same observable state. Such …

The association of biomolecules is the elementary event of communication in biology. Most
mechanistic information of how the interactions between binding partners form or break is …

Single-molecule tweezers, such as magnetic tweezers, are powerful tools for probing nm-
scale structural changes in single membrane proteins under force. However, the weak …