Cottrell Scholar Awards - 2015
Quantifying the Conformational Landscape of Maltose Binding Protein
Proteins are the molecules of life. There are tens of thousands of varieties in our bodies. They do everything from transporting oxygen in the bloodstream to attacking invading bacteria and viruses, to regulating our heartbeat. Proteins must be able to move and change their shapes in order to accomplish their tasks within the cell, be it a biochemical reaction or an interaction with another protein. Understanding the motions of proteins and the flexibility of protein shapes is crucial if we hope to understand the chemistry of living things.
Stefan Stoll, assistant professor of chemistry at the University of Washington, has received Cottrell Scholar funding to develop highly sensitive and accurate methods for measuring the flexibility of protein shapes.
To do so, he and his associates will rely on an advanced method called double electron-electron resonance (DEER) spectroscopy. DEER is a sensitive magnetic resonance technique similar to MRI used in medicine, except that it probes electrons within the proteins instead of hydrogen nuclei. With DEER experiments, it is possible to distinguish rigid proteins from flexible ones, and to quantify and visualize the flexibility.
“Like other techniques, DEER is not perfect,” Stoll said. “The sensitivity is ok, but not good enough to let us use it on all the proteins we are interested in. Also, the data we get are great, but we do not have validated ways of analyzing and modeling them accurately.” His endeavor is focused on massively increasing the sensitivity of this highly involved technology and to create a reliable measurement tool for other scientists.
Stoll is also using some of his Cottrell Scholar funding to design and produce an extensive series of brief lecture videos, a set of tutorial videos, and an online open-access textbook for undergraduates in physical chemistry. And he is integrating these videos into the course series at the University of Washington.