Folding and unfolding pathways are described for a ribosome-binding 3' cap-independent translation enhancer at the center of a conformational rearrangement that is implicated in the transition from translation to replication of an RNA virus.

Time-resolved transition metal ion fluorescence resonance energy transfer using a fluorescent, noncanonical amino acid donor and metal ion acceptor measures distances and distance distributions in proteins, allowing the equilibrium distributions among conformational states to be accurately determined.

The conformational switch of ABCG2 from the high substrate affinity inward-facing to a low substrate affinity outward-facing state is induced by nucleotide binding and accelerated by transported substrates.

Visualization of the real-time conformational transitions of the human voltage-gated proton channel hHv1 provided novel insights into how voltage and pH gradients modify the dynamic behaviors of channel structures to control proton flow across membrane.

Time-resolved tmFRET revealed structural and energetic changes induced by ligand binding with full agonist cAMP and partial agonist cGMP in the cyclic nucleotide-binding domain of the bacterial ion channel SthK.

Computer simulations explore the experimentally unknown S-protein structures, revealing novel drug binding sites.

Integration of structural bioinformatics and free-energy simulations reveals how a helicase switches its function from unwinding to rezipping DNA, during which a key metastable conformation is predicted and verified by single-molecule measurements.

Computations based on detailed atomic models explain how the ATP-driven sodium-potassium pump avoids transporting the wrong type of ions in order to maintain the physiological concentration of sodium and potassium ions across the cell membrane.

Compressive force spectroscopy of single molecules reveals that intra-protein forces underlie the long-distance coordination of structural changes within a cytotoxin during pore formation.

Computational and experimental evidence shows that the reaction catalyzed by adenylate kinase operates through a broad transition-state ensemble (TSE), utilizing protein conformational diversity to reduce activation entropy.