Graduate student Ashley Baxter will present
"A Sampling of the Use of Cryo-EM to Provide Structural Insights into Biomolecular Systems"
on April 3, 2018 at 4:10 PM in Neville Hall, Room 3.
Cyro-electron microscopy (cryo-EM) is a technique that structural biologists have been exploiting for decades to gain further insights into biochemical marcomolecules. Cyro-EM is a subset of electron microscopy, in that a beam of electrons is aimed at a sample and the nonscattered electrons are absorbed onto an electromagnetic plate, providing a shadow of an image of the sample. Techniques that have been employed in the past, such as X-ray crystallography and NMR, have limitations or shortcomings that cryo-EM can overcome. Cyro-EM allows scientists to visualize molecules in their native state and near-atomic resolution, which helps elucidate certain structural features. By broadening the structural understanding of biomacromolecules, their function can also be further understood. In this seminar, I will be highlighting three different protein macromolecules and how cryo-EM was used to give structural and thus functional insights into them. Firstly, I will talk about the structural differences of actin after it has been oxidized by a redox enzyme called Mical, and how these differences cause the instability of the protein. Secondly, I will discuss the structure of the catalytic subunit of oligosaccharyltransferase, which is the protein complex that catalyzes Nlinked glycosylation. Lastly, I will discuss the structure of the AMPAR ion channel, which plays a role in excitatory neurotransmission, and the global conformational shifts that occur upon ligand binding.
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