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Signaling in biological systems-- Insights from NMR
Presented by Prof. Ann McDermott
Hosted by Prof. Ruben Gonzalez, Jr.
Abstract:
Ion channels have been long recognized as one of the largest cell signaling superfamilies, underlying numerous critical health related phenomena. Allosteric processes in ion channels control their mean open time; by inactivating slowly (as a direct consequence of activation) the channel acts as a molecular timer. Solid state NMR experiments on full-length wild-type channel in proteo-liposomes provide evidence for a key role of evacuation of ions from the selectivity filter during inactivation, and thermodynamic coupling between channel activation and inactivation. NMR experiments have also identified residues that serve as “hotspots” for allostery. We examine an intermediate of the opening process and its conformational exchange processes.
Very high order oligomeric proteins, including amyloids, are increasingly reported to be involved in cell signaling in human health and disease. High order oligomer systems are associated with emergent properties such as force generation or multivalent binding. Studies using solid-state NMR address structural questions that are challenging by traditional methods.
Read more about Prof. McDermott here.
