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Nature Chemical Biology publishes research on protein kinase dynamic activation

The work of the Veglia Research Group, looking at a structural analysis of protein kinase A (PKA), was one of the featured articles in the October issue of Nature Chemical Biology journal.

Using nuclear magnetic resonance, X-ray crystallography, and thermodynamic measurements, the researchers analyzed the substrate recognition process of PKA, finding that entropy and protein dynamics play a prominent role. Read the complete article.

The article and featured research was written and conducted under the tutelage of Gianluigi Veglia, professor of Chemistry and Biochemistry at the University of Minnesota. Veglia credits the research of Larry Masterson, who is a postdoctoral research associate with the Veglia Research Group and who also was a graduate student under Veglia, and Masterson's efforts in getting the article published.

Other article authors include Tao Yu, a graduate student and research assistant at the University of Minnesota; Susan S. Taylor, a professor in chemistry and biology at the University of California, San Diego, and her lab associates, Cecilia Cheng, a graduate student who earned her doctorate in 2009, and Alexandr Kornev, a research specialist; and Marco Tonelli, research scientist and Varian instrumentation director at the National Magnetic Resonance Facility at Madison (NMRFAM), Department of Biochemistry, at the University of Wisconsin-Madison.

Veglia said that it took approximately four years to complete the research and write the article. This first-of-a-kind analysis of PKA highlights why nuclear magnetic resonance facilities and equipment is important to the University of Minnesota, he said.