MD-simulations reveal low- to high-affinity conformational shift of orthosteric site in the nicotinic acetylcholine receptor, offering insight into agonist roles in activation dynamics, and highlighting the utility of agonist efficiency.

A rapamycin-induced proximity assay enables rapid identification of optimal E3 ligases for target protein degradation in living cells, streamlining early-stage proteolysis targeting chimera development.

The manner in which protons control the conformational behaviour of mammalian peptide transporters is revealed through state-of-the-art molecular dynamics simulations supported by cell-based assays.

A neurofeedback training paradigm provides a new approach to manipulating physiologically relevant hippocampal replay.

Biochemical and structural investigations of the pH adaptability of mouse Acidic Mammalian Chitinase offer insights for designing enhanced enzyme variants that can function in both lung and gut.

CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.

A single conserved residue – histidine 12 – confers pH-sensitive DNA binding to the Salmonella Typhimurium SPI-2 transcriptional regulator SsrB, thereby regulating Salmonella virulence.

A genetically encoded sensor and a photocaged peptide together enable precise investigation of human glucagon-like peptide-1 receptor activation with high spatiotemporal resolution.

Benzene mapping simulations of envelope protein rafts from six different flaviviruses reveal a conserved cryptic site whose cluster of ionisable residues is likely responsible for orchestrating pH-dependent conformational changes during fusion, thereby representing an attractive target for antiviral development.