It is experimentally challenging to directly obtain structural information of the transition state
(TS), the high-energy bottleneck en route from reactants to products, for solution-phase …

The intricate coupling of mechanical force and chemical reactivity has been increasingly
revealed in recent years by force spectroscopy experiments on the thiol/disulfide exchange …

Single-molecule force-clamp spectroscopy offers a novel platform for mechanically
denaturing proteins by applying a constant force to a polyprotein. A powerful emerging …

The effect of mechanical force on the free-energy surface that governs a chemical reaction is
largely unknown. The combination of protein engineering with single-molecule force-clamp …

Mechanical force modifies the free-energy surface of chemical reactions, often enabling
thermodynamically unfavoured reaction pathways. Most of our molecular understanding of …

We use single-molecule force clamp spectroscopy (SMFCS) to explore the reactivity of tris (2-
carboxyethyl) phosphine (TCEP), 1, 4-dl-dithiothreitol (DTT) and hydrosulfide anion (HS−) …

The mechanism by which mechanical force regulates the kinetics of a chemical reaction is
unknown. Here, we use single-molecule force–clamp spectroscopy and protein engineering …

Recent force microscopy measurements on the mechanically activated cleavage of a protein
disulfide bond through reaction with hydroxide ions revealed that for forces greater than 0.5 …

The reduction of disulfides has a broad importance in chemistry, biochemistry and materials
science, particularly those methods that use mechanochemical activation. Here we show …

Mechanochemistry, in particular in the form of single-molecule atomic force microscopy
experiments, is difficult to model theoretically, for two reasons: Covalent bond breaking is not …