“Isn’t life a series of images that change as they repeat themselves?” – Andy Warhol
By Karen Kreeger
The derisive term “blobology” was once used to describe the not-so-clear knobby masses that could be discerned when trying to determine the shape of a protein. Now, with the latest advances in electron microscopy, almost every atom in a protein can be viewed and accounted for.
The improved technology that gives scientists this sharper view starts with a series of two-dimensional snapshots, like those above, of protein molecules flash-frozen in a thin layer of water. In this method, called cryo-EM, mathematical algorithms unite the pictures to bring the structure into sharp focus.
Getting a look at life’s essential molecules in this deeper way has improved scientists’ understanding of a range of human functions, from how kidney stones form to the connection between a breast cancer protein and lupus. Cryo-EM is even on the cusp of helping scientists better understand how natural products and drugs interact with neurons and other cells in the body. These insights could improve the treatment of cancer, heart disease, and kidney disorders. The technique, which won the 2017 Nobel Prize in Chemistry, is the core of Penn’s new Beckman Center for Cryo-EM, which held its ribbon cutting and inaugural symposium in late May of this year.
Vera Moiseenkova-Bell, PhD, faculty director of the Center and a professor of Systems Pharmacology and Translational Therapeutics, reflects on the power of the technology: “Although we are still refining the details of our images,” she said, “cryo-EM gives us an unprecedented view of how significant compounds interact with human proteins.”
Read more on the Penn Medicine News Blog.