Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.
The lipid kinase VPS34 complexes I and II are both activated by unsaturation of substrate and non-substrate lipids, curvature, electrostatics and polyphosphoinositides, which play roles in localisation and cellular function.
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.
Challenging a widespread model, biophysical and electrophysiological experiments suggest a new mechanism whereby complexins inhibit neurotransmitter release through electrostatic repulsion between their accessory helix and the membranes.
Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.