Browse our latest Structural Biology and Molecular Biophysics articles

NMR studies settle part of a long-standing debate about the mechanism used by the Hsp70 chaperone to recognize substrates.

Cryo-electron microscopy structures of human ribonucleotide reductase reveal molecular details of substrate selection and allosteric inhibition through assembly of its large subunit into a ring that excludes its small subunit.

NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.

Quantitative microscopy and theory show that the size of Xenopus laevis egg extract spindles is controlled by a spatially-regulated autocatalytic growth mechanism driven by microtubule-stimulated microtubule nucleation.

The primary cilia polycystin proteins, polycystin-1 and polycystin-2, affect cilia length in the kidney collecting duct epithelia, but only polycystin-2 is required for the functional ion channel in this organelle.

Spot-On is an easy-to-use website that makes a rigorous and bias-corrected modeling framework for analysis of single-molecule tracking experiments available to all.

The helical rod structure and dynamic spring-like properties of the type 1 pilus are evolutionarily fine-tuned for functioning in host-pathogen interactions during urinary tract infection and gut colonization.

Structural and functional characterization of an unanticipated mode of allosteric activity regulation in ribonucleotide reductases controlled by an ATP-cone in the radical-generating subunit.

MgADP binding to the high-affinity 'consensus' ATPase active site of SUR1 and remodeling of the L0-loop (lasso region) overrides tonic ATP inhibition of KATP channels.

The morphology and deformability of all blood cells can be measured continuously and with high throughput directly in whole blood without prior enrichment or separation.