Biochemical analysis on hetero-mutated c₁₀ subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.

The accumulation of its product, cytidine triphosphate, encourages the enzyme CTP synthetase (CtpS) to form large-scale polymers and inhibits the enzyme's activity.

Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.

A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy.

Cryo-EM studies reveal that incubation with ATP produces conformational intermediates of E. coli ATP synthase, in which the ε subunit is no longer in its autoinhibitory conformation.

Cryo-EM reveals atomic details of two membrane half-channels for translocation of protons that drive rotary catalysis in ATP synthase.

The dimer destabilizers cause a dimer-to-monomer equilibrium shift favoring the human thymidylate synthase monomer more degradable by the proteasome, thus breaking the long-standing link between inhibition and enhanced expression of the protein to fight cancer drug resistance.

The transmembrane shape of the F₁F_o ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.

Single-molecule F₁F_O studies show mutation-dependent pKa changes of both F_O half-channels, and proton translocation-dependent 11° ATP synthase-direction sub-steps, which support a Grotthuss proton transfer-dependent two-step F_O torque generating mechanism.

The mechanism of substrate binding cooperativity in human thymidylate synthase does not derive from millisecond dynamic interconversion between active and inactive conformations in solution, but instead results primarily from differential changes in faster side-chain motions (conformational entropy), facilitated by a disordered N-terminus.