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

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

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

The pivotal role of microfluidic technology in life science and biomedical research is now
widely recognized. Indeed, microfluidics as a research tool is unparalleled in terms of its …

Förster resonance energy transfer (FRET) and electron paramagnetic resonance (EPR)
spectroscopy are complementary techniques for quantifying distances in the nanometer …

The pore-forming toxin cytolysin A (ClyA) is expressed as a large α-helical monomer that,
upon interaction with membranes, undergoes a major conformational rearrangement into …

Single-molecule detection schemes offer powerful means to overcome static and dynamic
heterogeneity inherent to complex samples. However, probing biomolecular interactions …

The 303-residue cytolytic toxin ClyA forms a stable α-helical monomer. In the presence of
detergents or membranes, however, the protein makes a large conformational transition to …

Interactions between emerging nascent polypeptide chains and the ribosome can modulate
cotranslational protein folding. However, it has remained unclear how such interactions can …