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

Shifts in the balance between nucleotide-favorable and nucleotide-unfavorable conformations of myosin motors encode duty ratios and ADP release rates, demonstrating the power of an ensemble perspective for uncovering sequence-function relationships.

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.

Crowding and metabolites in a simulated cellular environment alter protein conformations, modulate interactions of functionally related proteins, and lead to significant dynamic heterogeneity.

Cryo EM and a custom subvolume refinement approach applied to mouse polyomavirus revealed the in vivo impact of polyomavirus capsid mutations on antiviral antibody immunoevasion and neurovirulence.

The physical interaction network encoded in the multi-domain protein native structure handles the trade-off between the fast, stable folding and the efficient, reliable function.

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.

With the removal of confounding artifacts, ribosome profiling can yield insight into the mechanism of protein synthesis in bacteria at high resolution.

A novel component of type III protein secretion systems involved in the assembly of the secretion machine is reported.