A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.

‘Optical tweezers’ measurements of single ribosomes and single mRNA molecules show that the translation rate depends exponentially on the applied force, and suggests that the ribosome functions as a Brownian ratchet.

Single-molecule experiments reveal the dynamics of transcription through a nucleosome with single-base-pair accuracy.

Deep penetration and transmission of mechanical force to regulate ER functions depends on not only the passive cytoskeletal support, but also the active actomyosin contractility, which is dispensable for mechanotransduction at the plasma membrane.

Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.

Single-molecule force and fluorescence spectroscopy reveal the structural states and dynamics of E. coli single-stranded DNA binding proteins and the energy landscape of the nucleo–protein complex.

The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.

The swimming behavior of E. coli is surprisingly robust against the natural variations in the number of flagella per cell.

The ability of an enzyme called XPD helicase to unwind the double helix is influenced by the DNA sequence and the availability of energy.

Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.