Manipulation of individual molecules with optical tweezers provides a powerful means of
interrogating the structure and folding of proteins. Mechanical force is not only a relevant …

Folding may be described conceptually in terms of trajectories over a landscape of free
energies corresponding to different molecular configurations. In practice, energy landscapes …

Protein folding occurs as a set of transitions between structural states within an energy
landscape. An oversimplified view of the folding process emerges when transiently …

Cellular DNA is continuously engaged in a molecular dance with many accessory proteins.
These proteins are responsible for orchestrating the storage, maintenance, and transfer of …

The use of force probes to induce unfolding and refolding of single molecules through the
application of mechanical tension, known as single-molecule force spectroscopy (SMFS) …

One of the most exciting developments in the field of biological physics in recent years is the
ability to manipulate single molecules and probe their properties and function. Since its …

Highlights•Optical tweezers provide a sensitive tool to probe structural dynamics.•Native and
non-native folding can be characterized in detail.•Effects of intermolecular interactions on …

The CRISPR-Cas9 nuclease has been widely repurposed as a molecular and cell biology
tool for its ability to programmably target and cleave DNA. Cas9 recognizes its target site by …

To understand membrane protein biogenesis, we need to explore folding within a bilayer
context. Here, we describe a single-molecule force microscopy technique that monitors the …

The timescale for the microscopic dynamics of proteins during conformational transitions is
set by the intrachain diffusion coefficient, D. Despite the central role of protein misfolding and …