Browse our latest Structural Biology and Molecular Biophysics articles

Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

Structure of MlaFB reveals how a small binding protein and the C-terminal tail on an ATPase subunit work together to regulate the assembly and function of an ABC transporter.

Multi-scale simulations reveal a potential, ATP-independent mechanism resulting in the formation of the long-living multi-droplet state by multi-valent, spacer-sticker proteins.

Computer simulations of model proteins with sticker-and-spacer architectures shed light on the formation of biomolecular condensates in cells.

The cysteine pair oxidation state in nDsbD acts as a ‘switch’ controlling the presence or absence of frustration in the active-site and determining the dynamic behavior of the cap loop.

The structure of the chromatin remodeller CHD4 bound to a nucleosome reveals differences to the known Chd1-nucleosome complex and maps cancer mutations.

First structural view of a substrate-bound PIKK (PI3K-related-kinase) by cryo-EM explains phosphorylation specificity toward a short amino-acid motif shared across the PIKK family and rationalizes PIKK auto-inhibition by regulatory domain.

The ciliate mitoribosome structure provides new insights into the diversity of translation and its evolution.

The lipid kinase VPS34 complexes I and II are both activated by unsaturation of substrate and non-substrate lipids, curvature, electrostatics and polyphosphoinositides, which play roles in localisation and cellular function.