Optical tweezers articles from across Nature Portfolio

Protein complexes are essential for cell function. Here, authors show that paired ribosomes can help each other’s nascent chains fold correctly, enabling proper dimer assembly and preventing misfolding, using lamin as a model system.

Single-stranded DNA-binding proteins protect exposed DNA during replication but create potential barriers for polymerases. Here, the authors reveal that DNA polymerase actively and sequentially displaces stationary SSB proteins. The SSB C-terminal tail facilitates this process by reducing energy barriers for displacement to ensure DNA replication.

Chromosomes are coated in proteins and RNA called the mitotic chromosome periphery. Here, broadband microrheology analysis has shown that this coat has dynamic, liquid-like properties and provides an external structural constraint.

The human mitochondrial helicase Twinkle is essential for maintaining mitochondrial DNA. Here, the authors combine biochemical and single-molecule approaches to show how Twinkle’s real-time kinetics are regulated by its amino and carboxyl terminal domains, revealing a key auto-regulatory mechanism.

DNA polymerase engages with DNA in various ways during replication. Using mechanical DNA manipulation and single-molecule fluorescence the authors show that replication is dynamic. Bursts of polymerase activity interspersed with protein exchanges and a memory effect can be observed, during replication.

This study presents an image processing-based stage height control and optical trap dithering technique to detect protein-protein interactions. It was used to show that the MT binding rate for KIF5B has a strong spatial and motor length dependence.

Polymer physics, comparing ways to assess chromatin structure and taking in tales at the Italian seaside.

Germanium nanoparticles enable optical trapping at high spatiotemporal resolution.