Allosteric modulation of BK channels, vital for the physiology of nerve, muscle and endocrine cells, is determined by direct coupling between gating ring RCK1 domains and the voltage sensor function.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.

Human subjects actively adjust the acquisition of sense data based on how their bodily cycles alter their senses, i.e., sensing tactile stimuli for longer periods when concurrent physiological signals are present vs. sensing for shorter periods when these are quiescent.

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.

Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

The use of a conformation-selective inhibitory nanobody provides critical information on MelB at a low-sugar affinity inward-facing Na⁺-bound state for establishing the mobile barrier and substrate-releasing mechanisms.

Efficiency measures the fundamental link between agonist binding and protein conformational change, and in nicotinic receptors has 5 values that calibrate energy changes in the induced fit that triggers activation.

Motor context and mechanosensory feedback together influence how flies control head movements during visually guided flight maneuvers.

The anchoring properties of Ca_V β2 subunits to the plasma membrane determine the biophysical states of Ca_V2.2 channels by regulating PIP₂ coupling to the nonspecific phospholipid-binding site in the I–II loop.