Rebecca Eels shared a bit about her complex work with cells at the Lions meeting.

By Kurt Karr, Vinton Lions Club

Rebecca Eells was the speaker at the Vinton Lion’s club meeting last Wednesday. Rebecca is pursuing a Ph.D. in Molecular Biophysics at Carnegie Mellon University in Pittsburgh. Rebecca received her bachelor’s in physics from Vassar. She is the daughter of Gwen and Don Eells.
The Lions wish to express their appreciation for the valiant effort Rebecca made to present her work to our non-scientific audience, but alas, no one left the meeting believing their future was in biophysics.
Our bodies produce more than 20,000 proteins that regulate processes within our bodies, from digestion to transporting oxygen. The function of proteins not only depend on their amino acid composition, but also on the shape of the protein strand. The electrical charge of each amino acid in the protein and the way those charges attract or repel other amino acids within the strand determine the shape. Rebecca’s research is at the intersection of physics, chemistry, and molecular biology.
“I spend most of my days in fairly mundane lab work,” explained Rebecca. “I start by washing and cleaning slides, then preparing them for the next series of experiments. A lot of my time is spent with pipettes, prepping slides and putting them in a non-descript black box. Analyzing the data we generate is what takes the most time.”
Rebecca’s work holds promise in the development of new drug therapies for many of our worst diseases. Her current work relates to the HIV and its ability to infect a cell, hijack the cell’s machinery to make more viruses, and send the new virus cells out into the body. She shared that HIV is so incredibly adaptable that missing just one day’s prescribed medication can result in the virus having resistance to the patient’s drug regimen.
Complicating the work of researchers like Rebecca is the potential for unwanted side-effects caused by the medicines they create. Often those side-effects are caused because a protein helpful in stopping a virus from spreading might also bond in a way that prevents healthy processes from occurring.
Asked about her future, Rebecca shared that hopes for a career working in research exploring new pharmaceuticals.

Our bodies make roughly 20,000 different kinds of proteins, from the collagen in our skin to the hemoglobin in our blood. Some take the shape of molecular sheets. Others are sculpted into fibers, boxes, tunnels, even scissors.
A protein’s particular shape enables it to do a particular job, whether ferrying oxygen through the body or helping to digest food.
Scientists have studied proteins for nearly two centuries, and over that time they’ve worked out how cells create them from simple building blocks. They have long dreamed of assembling those elements into new proteins not found in nature.
But they’ve been stumped by one great mystery: how the building blocks in a protein take their final shape. David Baker, 55, the director of the Institute for Protein Design at the University of Washington, has been investigating that enigma for a quarter-century.