Abstract
GLIC, a proton-gated cation-selective channel, is a prokaryotic homologue of the pentameric Cys-loop receptor ligand-gated ion channel family. The conformational changes in the extracellular domain (ECD) and transmembrane domain (TMD) during gating of this receptor channel family were inferred from X-ray structures at pH4 (open) and pH7 (closed), but remain elusive under native conditions. Here, we used high-speed atomic force microscopy (HS-AFM) combined with a buffer exchange system to directly study receptor channel gating on the single molecule level in the membrane in physiological buffer and at ambient temperature and pressure.
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