A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.

A combination of single-molecule imaging and an in vitro model of the cell cortex has allowed the interactions between actin filaments and filaments made of myosin II to be studied in detail.

An interaction between two proteins enables the spindle—the structure that segregates chromosome pairs during mitosis—to change size as cells divide.

The transport of proteins along flagellar microtubules generates the force that enables flagella to propel cells across surfaces.

Computer simulations reveal that viral nucleic acids have an ideal structure for being packaged into outer protein shells called capsids.

C-terminal phosphorylation of the lipid phosphatase PTEN drives a reduction in membrane affinity and leads to a more compact conformation that involves a C2 domain-tail interaction.

The structural basis for Her2's role as a dedicated heterodimerization partner for other EGFR family receptors is elucidated with long-timescale atomistic simulations.

The basal body of the type-III secretion system of Yersinia enterocolitica within bacterial membranes shows elasticity and is longer than related isolated systems.

Structural studies reveal the mechanism by which a HECT E3 ubiquitin ligase carries out E2-to-E3-to-substrate ubiquitin transfer and prioritizes target lysines for ubiquitination.