BACKGROUND Biomolecular mechanisms are typically inferred from static structural
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …

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

Probing non-equilibrium dynamics with single-molecule spectroscopy is important for
dissecting biomolecular mechanisms. However, existing microfluidic rapid-mixing systems …

The development of lab-on-a-chip technology and its applications in biochemical and
biomedical analyses has, during the last two decades, led to the potential realisation of …

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

Single-molecule fluorescence microscopy is uniquely suited for detecting transient
molecular recognition events, yet achieving the time resolution and statistics needed to …

Single-molecule methods have become widely used for quantifying the conformational
heterogeneity and structural dynamics of biomolecules in vitro. Their application in vivo …

Highlights•Single molecule FRET experiments determine average transition path
times.•Observed times are extremely close to those found in all-atom MD simulations.•Times …

Highlights•The potential impact of multi-color single-molecule FRET imaging.•Key
requirement: ultra-stable fluorophores spanning the visible spectrum.•Intramolecularly …

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins
are very common and instrumental for cellular signaling. Recently, a number of studies have …