Magnetic tweezers articles from across Nature Portfolio

Kwak et al. report that adherens junctions organize membrane microdomains, leading to lipid-dependent γ-secretase recruitment and size-dependent protein segregation, excluding full-length Notch receptor.

Wang et al. show how genetic sequence and base modifications can be detected simultaneously on single molecules of both DNA and RNA using magnetic tweezers. They also demonstrate an amplification-free CRISPR/Cas9-based strategy for isolating target regions from native DNA and apply this approach to the isolation of targets from E. coli and human genomic DNA.

Bacteria use thioester-bond-containing proteins to covalently bind to host surfaces and withstand large mechanical shocks. Now, thioester bond reactivity has been shown to be force-dependent: forces >35 pN inhibit bond cleavage by primary amine ligands, whereas forces <6 pN enable reversible reformation. This force-modulated thioester bond reactivity could potentially enable bacterial mobility and a route by which they optimize infection.

Single molecule force measurements have shed light on dynamic biological events, but rare events escape notice owing to low throughput of the methods. Here, the authors combine an array of magnetic tweezers with lateral flow to increase throughput 100-fold, and detect rare DNA breaks induced by gyrase.

Mechanically stable specific heterodimerization formed with reversible bonds are used as a molecular anchorage in single-molecule force spectroscopy studies with unique mechanical properties. Here authors develop a variety of heterodimerization molecular systems with a range of mechanical stability from a set of recently engineered helix-heterotetramers.

Membrane proteins are embedded in the lipid bilayer of the plasma membrane and their function in this context is often linked to their specific location and dynamics within the membrane. Here authors report the use of fluorescent magnetic nanoparticles to track membrane molecules and to manipulate their movement and pull membrane components laterally through the membrane with femtonewton-range forces.