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

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

Single-molecule FRET (smFRET) is a versatile technique to study the dynamics and function
of biomolecules since it makes nanoscale movements detectable as fluorescence signals …

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

Fundamental properties of light unavoidably impose features on images collected using
fluorescence microscopes. Accounting for these features is often critical in quantitatively …

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

Fluorescence correlation spectroscopy (FCS) is a flexible and widely used tool routinely
exploited in vivo. While FCS provides estimates of dynamical quantities, such as diffusion …

We present a unified conceptual framework and the associated software package for single-
molecule Förster resonance energy transfer (smFRET) analysis from single-photon arrivals …

Fluorescence time traces are used to report on dynamical properties of molecules. The basic
unit of information in these traces is the arrival time of individual photons, which carry …

For many classes of biomolecules, population-level heterogeneity is an essential aspect of
biological function─ from antibodies produced by the immune system to post-translationally …