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

Feynman commented that “Everything that living things do can be understood in terms of the
jiggling and wiggling of atoms”. Proteins can jiggle and wiggle large structural elements …

Single-molecule Förster-resonance energy transfer (smFRET) experiments allow the study
of biomolecular structure and dynamics in vitro and in vivo. We performed an international …

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 …

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

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

When described by a low-dimensional reaction coordinate, the folding rates of most proteins
are determined by a subtle interplay between free-energy barriers, which separate folded …

Intrinsically disordered proteins often form dynamic complexes with their ligands. Yet, the
speed and amplitude of these motions are hidden in classical binding kinetics. Here, we …

The functional cycle of many proteins involves large-scale motions of domains and subunits.
The relation between conformational dynamics and the chemical steps of enzymes remains …

Membrane protein biogenesis poses acute challenges to protein homeostasis, and how they
are selectively escorted to the target membrane is not well understood. Here we address this …