The Hibbs Lab is pursuing atomic-scale mechanisms of synaptic proteins, with a current focus on ligand-gated ion channel structure and function. We are fascinated by how these complex molecules respond to the binding of a small chemical neurotransmitter by triggering the opening of an intrinsic ion conduction pathway >50 Å away. This conformational conversion allows for diffusion-limited rates of ion flux and occurs on the millisecond timescale. We further seek to probe mechanisms of ion selectivity and allosteric modulation, with a long-term goal of better informing rational therapeutic design for neurological disorders and addiction. We employ a multidisciplinary approach encompassing molecular biology, protein biochemistry, pharmacology, x-ray crystallography, cryo-electron microscopy, and electrophysiology. Recent work from the lab has explored the structural biology of heteromeric nicotinic receptors and GABAA receptors both by crystallographic and cryo-EM approaches.