Browse our latest Structural Biology and Molecular Biophysics articles

Cryo-EM structures reveal that MICU1-MICU2 operates like a regulatable toxin to block the pore of the mitochondrial calcium uniporter and confer Ca²⁺-dependent control.

Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

Cryo-EM analysis of human ZnT8 reveals a large conformational change of TMD during the transport cycle.

Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.

Structure of the Mrp antiporter, an ancestor of respiratory complex I, suggests a mechanism of coupling between cation and proton translocation, applicable to a large family of related membrane proteins.

The in-depth structural and functional work provide a deeper understanding as to how the epithelial sodium channel is a heteromeric ion channel that is regulated by Na⁺ and proteolysis.

In vitro reconstitution of the core focal adhesion proteins talin and vinculin with actin reveals lipid-dependent release of autoinhibition.

Changes to cellular protein homeostasis reveal widespread advantageous effects of destabilizing mutations, opening the possibility to switch mutational landscapes back-and-forth from permissive to restrictive.

Efficient nuclear transport of very large biomolecules, relevant for viral transport, scales non-linearly with size and its kinetics can be explained by a simple two-parameter energetic model.

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.