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) …

Single-molecule force spectroscopy with the atomic force microscope provides molecular
level insights into protein function, allowing researchers to reconstruct energy landscapes …

Simple Summary Proteins are composed of compact domains, often of known three-
dimensional structure, and natively unstructured polypeptide regions. The abundant cold …

Transition paths of macromolecular conformational changes such as protein folding are
predicted to be heterogeneous. However, experimental characterization of the diversity of …

Correct protein folding is essential for the health and function of living organisms. Yet, it is
not well understood how unfolded proteins reach their native state and avoid aggregation …

Electrosprayed protein ions can retain native-like conformations. The intramolecular
contacts that stabilize these compact gas-phase structures remain poorly understood …

One of the major challenges in modern biophysics is observing and understanding
conformational changes during complex molecular processes, from the fundamental protein …

The perturbation of a protein conformation by a physiological fluid flow is crucial in various
biological processes including blood clotting and bacterial adhesion to human tissues …

Conspectus The function of proteins as biological nanomachines relies on their ability to fold
into complex 3D structures, bind selectively to partners, and undergo conformational …

Cold shock protein (Csp) is a typical two-state folding model protein which has been widely
studied by biochemistry and single molecule techniques. Recently two-state property of Csp …