University of Wisconsin–Milwaukee

Laura Hunt


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Feb 22, 2010 
Seventh UWM physicist gets CAREER Award
Marius Schmidt
Marius Schmidt

Marius Schmidt, a physicist at the University of Wisconsin–Milwaukee (UWM), has received an Early Career Development (CAREER) Award from the National Science Foundation (NSF), which will support his work on imaging proteins as their atomic structure changes during biochemical reactions. The work could ultimately provide insights for new drug discovery.

Schmidt is the third UWM researcher to be awarded a CAREER grant in the last year, and the seventh member of UWM’s Department of Physics to receive one.

CAREER grants are the NSF’s most prestigious grants for younger researchers. They support the career development of teacher-scholars who are most likely to become the academic leaders of this century. Of the 17 UWM CAREER grant winners named in the last 15 years, all are still active faculty members.

“It is a singular accomplishment for UWM to have so many physicists in our mid-sized department honored with such an influential grant,” says Richard Meadows, dean of the UWM College of Letters and Science. “It also illustrates the department’s ability to identify and recruit young faculty who are able to compete at the highest levels.”

Schmidt, an assistant professor, will use the more than $900,000 grant, awarded over five years, to examine the structural changes of proteins that carry out essential functions of life by catalyzing biochemical reactions.

A time-series on the L29W myoglobin mutant measured in 2005.

A substantial reorganization of the protein’s atomic structure occurs during these reactions, such as those that allow some bacteria to glow or react to light.Using an X-ray diffraction technique called time-resolved crystallography, Schmidt will explore two biological processes involving color-changing in molecules exposed to light.

Time-resolved crystallography can image an ensemble of molecules in four dimensions – three spatial dimensions and time. By adding and varying temperature, Schmidt can see all the changes as they happen, obtaining a comprehensive view of how the protein accomplishes its photoactive work.

“In the simplest terms, you are flipping atoms in the protein, which leads to the color changing,” says Schmidt. “You want to directly observe the atoms that are flipping and how it’s happening because there are many stages that occur.”

The research could lead to a rational design of optical switches that could be used in biophysical research. Replicating the work of proteins is also an important aspect of new drug discovery.

Schmidt earned his doctorate at Technische Universität München, Garching, Germany. Before joining the UWM Physics Department in 2007, he was a research associate in the Department of Biochemistry and Molecular Biology at the University of Chicago and a scientist in the Physics Department at Technische Universität München.

Lei (Leslie) Ying, an associate professor in Electrical Engineering and Computer Science, and Stefan Schnitzer, an associate professor in Biological Sciences, were awarded CAREER grants last summer.