In potassium-dependent NTPases, insertion of the activating potassium ion into the active site leads to rotation of the gamma-phosphate yielding a near-eclipsed, catalytically productive conformation of the triphosphate chain.

The identification of a conserved α-helical domain in monkeypox virus H3 protein as critical for heparan sulfate binding unveils a novel therapeutic target, validated through AI and molecular dynamics simulations, offering potential for broad-spectrum antiviral development.

Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl^- and H⁺ ions move when crossing biological membranes.

The orientation of the TCR extracellular domain is highly variable and coupled to characteristic structural changes throughout the TCR - CD3 complex.

The conformation of an isoleucine gate located along the TM6 segment on the intracellular side below the selectivity filter is a critical component leading to a non-conductive state in the C-type inactivation process of K⁺ channels.

Computer simulations explore the experimentally unknown S-protein structures, revealing novel drug binding sites.

Viral evolution can lead to mutations that render specific glycosylation sites dispensable for folding and for supporting the protein's function, allowing changes in the shield, and in the immunogenic profile.

Structures of multiple states of two dicarboxylate transporters explain the conformational changes needed for substrate import.

An entropy switch controls the Aurora B autoactivation process through two distinct kinetic steps of phosphorylation.

A combination of high-resolution structure determination, electrophysiology, and MD simulations reveal fundamental insight into the molecular function of voltage-gated chloride channels.