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Tyler Gerczak, a materials scientist at Oak Ridge National Laboratory, is focused on post-irradiation examination and separate effects testing of current fuels for light water reactors and advanced fuel types that could be used in future nuclear systems. Credit: Carlos Jones/Oak Ridge National Laboratory, U.S. Dept. of Energy

Ask Tyler Gerczak to find a negative in working at the Department of Energy’s Oak Ridge National Laboratory, and his only complaint is the summer weather. It is not as forgiving as the summers in Pulaski, Wisconsin, his hometown.

Illustration of the intricate organization of the PKA structure, wherein different parts of the protein are connected through elaborate hydrogen bonding networks (dashed yellow lines), glued together by the hydrophobic assemblies (light blue and orange volumes)—all working together to build the functional active site. Insert shows protonation of the transferred phosphoryl group (cyan mesh) and its many interactions with water and the active site amino acid residues. Credit: Jill Hemman/ORNL

OAK RIDGE, Tenn., March 20, 2019—Direct observations of the structure and catalytic mechanism of a prototypical kinase enzyme—protein kinase A or PKA—will provide researchers and drug developers with significantly enhanced abilities to understand and treat fatal diseases and neurological disorders such as cancer, diabetes, and cystic fibrosis.