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A multiscale modeling approach reveals how the energy from ATP hydrolysis is used by Hsp70 chaperones to remodel the conformation of their substrates through a novel force-generating mechanism.

Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.

Sodium selectivity of acid-sensing ion channels is mediated by negatively charged side chains and not by a size-exclusion mechanism.

cryo-EM reveals the properties of distinct conformations occupied during activation of the lipid scramblase nhTMEM16 and provides new insights into its interactions with the lipid environment.

A new combined mechanism explains how GTP binding by tubulin is linked to its dynamics and energetics in solution and why GTP-induced flexibility, and not the tubulin conformation as such, drives microtubule assembly.

Using state-specific contacts inferred from coevolving residue pairs enables us to build models of the various conformational states along the sugar porter functional cycle and reconstruct the free-energy landscape of the process.

Across a physiological span of ATP-free energy, leukemic mitochondria primarily consume, rather than produce, ATP.

Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.

The brown planthopper has evolved a highly adaptive oviposition strategy by exploiting caterpillar-induced plant volatiles that provide safe havens for its offspring.