A summary of the current “state-of-the-field” of single-molecule FRET used for probing biomolecular structural dynamics.

The viscous hydraulics of contracting endoplasmic reticulum networks challenge common solute transport theories, suggesting the contraction of peripheral sheets as a plausible driving mechanism.

Orthologous proteins that continuously maintain the same molecular function do not usually diverge beyond a certain level of sequence and structural similarity.

An experimentally constrained model shows that Escherichia coli faces fitness trade-offs in chemotaxis behaviors, and that adaptation of phenotypic diversity through altered gene regulation permits populations to resolve these trade-offs.

Transcriptional activation domains achieve rapid, dynamic, specific interaction with Mediator through binding of an unstructured peptide to multiple hydrophobic surfaces without particular amino acid side chain interactions.

Noise in a signaling network comprising thousands of molecules shapes diversity across cell populations and generates giant temporal fluctuations at the single-cell level.