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Structural studies of HypF-N Amyloid Fibril Formation - 20 October 2020

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Speaker: Dr James Jarvis, NMR Facility Manager, King's College London

Host: Sasi Conte

HypF-N protein is the N-terminal 91 amino acids of the E.coli acylphosphatase enzyme HypF. HypF-N has recently attracted significant interest as a model system for amyloid toxicity. It is possible to form two different types of amyloid oligomers and fibrils from HypF-N under well-defined conditions; those which are toxic to cultured cells, and those which are not. This provides a unique opportunity to compare properties of the amyloid oligomers and fibrils of the two systems in order determine the biochemical, structural and molecular basis of toxicity of the amyloid species, with important implications for the molecular mechanism of toxicity for amyloid diseases in general.

In this talk, results aimed at determining structural features of different species on the HypF-N amyloid pathways are presented. Soluble, oligomeric and fibrillar species are characterised using a combination of solution-state and solid-state NMR, cryo-EM and FRET. We present novel solution-state and solid-state NMR assignments of species on a previously undescribed fibrilisation pathway for HypF-N.


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