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How Elastic Are Proteins? UB Physics Professor Receives CAREER Award to Find Out

Research goal is a tabletop system that detects protein binding

Release Date: May 20, 2004

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Andrea Markelz has received a prestigious CAREER award from the National Science Foundation to continue her research on proteins.

BUFFALO, N.Y. -- Andrea Markelz, Ph.D., assistant professor of physics in the University at Buffalo College of Arts and Sciences, has received a prestigious Faculty Early Career Development Award from the National Science Foundation to develop a technique for measuring the elasticity -- or "bounciness" -- of biomolecules, such as proteins, using ultrafast optical methods.

The grant provides $600,000 to Markelz' research group over the next five years.

According to the NSF, the CAREER program recognizes and supports the early career-development activities of teacher-scholars "who are most likely to become the academic leaders of the 21st century."

Markelz' research is geared toward understanding how protein flexibility affects protein function and developing a tabletop system that can perform a universal, high-throughput assay to detect protein binding.

Such an assay is a high priority for the pharmaceutical industry, where combinatorial screening can result in hundreds or thousands of drug leads. The work also has applications to biosensor development.

Other techniques that may be able to measure protein flexibility include nuclear magnetic resonance (NMR) and neutron beam experiments, neither of which can be described as "tabletop," Markelz explained.

"There are no tabletop systems that do this," she said. "Ours does. Conceivably, a biochemist or geneticist could have this system in their labs, allowing them to rapidly determine the change in flexibility with binding or environmental change."

Markelz' group is one of a handful in the world examining proteins from a materials perspective, looking at their bulk, or physical, characteristics, using a technique called terahertz time domain spectroscopy.

"Recently, scientists have come to recognize that to understand how proteins function, you have to include their flexibility," she said.

By changing their flexibility, she explained, you can change their ability to function.

"For example, in some cases, proteins become less flexible when they are bound to another molecule, and this actually provides a method of feedback control for protein production," she explained.

Research published by Markelz' group last year in Biophysical Journal established that the technique it developed is, indeed, sensitive to the functional state of a photoactive protein, bacteriorhodopsin, which is closely related to rhodopsin, the protein responsible for vision.

As part of the CAREER grant, Markelz also will establish an educational program between UB, the Buffalo Public Schools and the Buffalo Museum of Science aimed at attracting more females and other under-represented groups into the sciences.

Markelz added that biophysics is becoming a critical research strength for UB with numerous centers, departments and individual researchers involved in studying quantitative aspects of biophysical phenomena.

"This community is growing and very collegial," she said. "My graduate students and I have been able to discuss research with UB colleagues spread over a wide range of disciplines with common research interests and goals. It is a wonderful environment in which to pursue this work."

Markelz, who holds adjunct appointments in UB's departments of electrical engineering and structural biology, lives in East Amherst.

Media Contact Information

Ellen Goldbaum
News Content Manager
Medicine
Tel: 716-645-4605
goldbaum@buffalo.edu
Twitter: @UBmednews