All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Highlights•The accuracy of physical models used in protein-folding simulations is
assessed.•This assessment is based on data from very long molecular dynamics …

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 …

Optical tweezers are tools made of light that enable contactless pushing, trapping, and
manipulation of objects, ranging from atoms to space light sails. Since the pioneering work …

Nuclear magnetic resonance spectroscopy is a powerful tool for the structural analysis of
organic compounds and biomolecules but typically requires macroscopic sample quantities …

Protein–protein association is fundamental to many life processes. However, a microscopic
model describing the structures and kinetics during association and dissociation is lacking …

We extract the folding free energy landscape and the time-dependent friction function, the
two ingredients of the generalized Langevin equation (GLE), from explicit-water molecular …

A goal in the kinetic characterization of a macromolecular system is the description of its
slow relaxation processes via (i) identification of the structural changes involved in these …

We introduce self-assembled nanoantennas to enhance the fluorescence intensity in a
plasmonic hotspot of zeptoliter volume. The nanoantennas are prepared by attaching one or …

The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …