Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.

Cryo-electron microscopy structures, combined with biochemical experiments, show how the E. coli F element-encoded TraR protein regulates transcription initiation by altering RNA polymerase conformation and conformational heterogeneity.

Single molecule DNA-binding trajectories and deterministic modeling analyses demonstrate a functional role for high energy partly folded states in Transcription Activator-Like Effectors that could improve future TALEN design.

Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.

The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.

The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.

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.

Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.

Cryo-EM structures of human MCU-EMRE-MICU1-MICU2 complex in the apo and Ca²⁺-bound states reveal how MICU1 and MICU2 impart their gating function to the mitochondrial calcium uniporter.

Despite size heterogeneity, an epitope-resurfaced mature-form dengue VLP has the potential to induce quaternary structure-recognizing broad cross-reactive neutralizing antibodies.