Optical microscopy has for centuries been a key tool to study living cells with minimum
invasiveness. The advent of single molecule techniques over the past two decades has …

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

Molecular communication in biology is mediated by protein interactions. According to the
current paradigm, the specificity and affinity required for these interactions are encoded in …

High-resolution, multiplexed experiments are a staple in cellular imaging. Analogous
experiments in animals are challenging, however, due to substantial scattering and …

The use of dynamic, self-assembled DNA nanostructures in the context of nanorobotics
requires fast and reliable actuation mechanisms. We therefore created a 55-nanometer–by …

Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which
makes their structural characterization challenging. Although challenging, characterization …

Forces in biological systems are typically investigated at the single-molecule level with
atomic force microscopy or optical and magnetic tweezers, but these techniques suffer from …

Single-molecule fluorescence resonance energy transfer (smFRET) is one of the most
general and adaptable single-molecule techniques. Despite the explosive growth in the …

Chromosomes of a broad range of species, from bacteria to mammals, are structured by
large topological domains whose precise functional roles and regulatory mechanisms …