Browse our latest Structural Biology and Molecular Biophysics articles

Motif length plays a critical role in the specification of biological function within a conserved family of RNA-binding proteins.

Meiotic chromosome axis 'core' proteins from fungi, plants, and mammals form a conserved filament architecture, and use a common mechanism to recruit HORMAD proteins for meiotic recombination control.

A functionally conserved inactivation gate in the inner helix of Piezo channels controls the majority of the inactivation process via a hydrophobic mechanism.

Specific attachment of molecularly defined gold nanoparticles enables precise localization, critical for structural studies in vivo, of proteins of unknown structure within the cellular milieu by cryo-electron tomography.

Biochemical analysis reveals molecular mechanisms underlying the activation of the mitochondrial Ca²⁺ uniporter by intracellular Ca²⁺ signals.

Structural and biochemical analysis of human CtIP provides new insights into DNA break recognition, binding and bridging during homologous recombination.

Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.

There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

The range of barrel-shaped proteins found in the outer membrane of certain bacteria evolved through multiple pathways.

A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.