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.

The manner in which protons control the conformational behaviour of mammalian peptide transporters is revealed through state-of-the-art molecular dynamics simulations supported by cell-based assays.

Ligands with different efficacy profiles shift the free energy landscape of the beta2 adrenergic receptor activation and stabilize diverse active-like states via the switch of microswitches lining an allosteric pathway.

Molecular simulations can capture key aspects of the conformational exchange in a protein.

Computational methods based on both sequence and structure show evidence that tyrosine kinases are energetically biased to populate the 'DFG-out' type-II inhibitor binding conformation relative to serine/threonine kinases.

Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.

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.

Extensive molecular dynamics simulations enhanced by advanced sampling techniques give a detailed view of p38α canonical activation mechanism, which reveals novel key electrostatic interactions that are put in context of existing experimental data.

Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl^- and H⁺ ions move when crossing biological membranes.