‘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.

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.

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 energy landscape of SNARE folding and assembly is optimized for efficient stage-wise membrane fusion.

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.

Single-molecule methods reveal that cytidine triphosphate promotes DNA condensation specifically at bacterial centromeres by facilitating one-dimensional diffusion of ParB from parS sites.

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

Folding and unfolding pathways are described for a ribosome-binding 3' cap-independent translation enhancer at the center of a conformational rearrangement that is implicated in the transition from translation to replication of an RNA virus.

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.

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