On 28th November OxTalks will move to the new Halo platform and will become 'Oxford Events' (full details are available on the Staff Gateway).
There will be an OxTalks freeze beginning on Friday 14th November. This means you will need to publish any of your known events to OxTalks by then as there will be no facility to publish or edit events in that fortnight. During the freeze, all events will be migrated to the new Oxford Events site. It will still be possible to view events on OxTalks during this time.
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The talk will be live-streamed through the Oxford University Scientific Society’s YouTube channel, Facebook age, and Twitter account.
Proteins mediate the critical processes of life and beautifully solve the challenges faced during the evolution of modern organisms. Our goal is to design a new generation of proteins that address current-day problems not faced during evolution. In contrast to traditional protein engineering efforts, which have focused on modifying naturally occurring proteins, we design new proteins from scratch based on Anfinsen’s principle that proteins fold to their global free energy minimum. We compute amino acid sequences predicted to fold into proteins with new structures and functions, produce synthetic genes encoding these sequences, and characterize them experimentally. SARS-CoV-2 provided a test of the relevance of these methods to real-world challenges. In this talk, I will describe the de novo design of SARS-CoV-2 candidate diagnostics, therapeutics, and vaccines: designed switches which luminesce in the presence of antiviral antibodies, designed 55 residue proteins that bind to the Spike with picomolar affinity and block viral infection, and nanoparticle immunogens which elicit much higher yields of neutralizing antibodies in animals than the Spike trimer that is the basis of most current vaccine trials. I will close by describing the status of getting these into the clinic, and lessons for combatting future pandemics.