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UAlbany Researcher Leads Team in Development of Innovative Approach to Mapping Protein Interactions
American Diabetes Association awards Alex Shekhtman $800,000 to study proteins in Type II Diabetes

Contact: Catherine Herman (518) 437-4980

ALBANY, N.Y. (March 9, 2006) -- A team of researchers led by led by the University at Albany's Alex Shekhtman has developed a novel technique to observe protein interactions in living cells using NMR (nuclear magnetic resonance) spectroscopy. In a paper published in the February issue of Nature Methods, "Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)," the team describes an innovative general approach to study how biological molecules interact with each other inside the cells. Information about protein-protein interactions is of vital significance to understand the organisms in health and disease, such as diabetes.

"Interactions between protein molecules determine how cells behave in the human body," said Shekhtman, who leads the University's laboratory of NMR structural biology. "When protein interactions go awry, the cells function improperly, resulting in a number of common diseases including cancer and diabetes, thus underscoring the importance of understanding how proteins interact. We developed an approach which allows us to get atomic resolution information about relevant biological interactions under the native cellular conditions."

The team observed how separate atoms constituting interacting molecules are engaged during biomolecular interactions. Employing the power of UAlbany's newly installed 700 MHz NMR spectrometer, the researchers were able to resolve signals originating from the interacting molecules and separate them from the rest of the cellular content. The NMR spectrometer was critical for this research since it provided enough sensitivity to monitor biological interactions inside the living cells.

Interactions between protein molecules result in changes in their structure; these specific changes, in turn, regulate how the cells behave. The researchers recognized that they could observe such changes inside living cells using NMR spectroscopy that allow scientists to determine the structure of a protein. The technique, named STINT-NMR for STructural INTeractions, uses bacteria to first make a specifically marked protein that can be seen using NMR spectrometer, followed by a second, unmarked protein that binds to the first; the unmarked protein is invisible to the NMR spectrometer. When the two proteins bind to one another, the NMR signal changes, reflecting the changes in the structure of the marked protein. By reversing the order of the experiment, the changes in both proteins can be seen. The team also suggests that their approach should work just as well for three or more interacting proteins.

This technique provides a structural foundation for molecular biological studies of cells in health and disease. Shekhtman's laboratory has received an $800,000 award from the American Diabetes Association to study protein-protein interactions involved in the development of type II diabetes. Shekhtman's team includes David Burz, post-doctoral researcher at the University at Albany and Kaushik Dutta and David Cowburn from the New York Structural Biology Center.


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