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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.

Radiochemical technicians David Denton and Karen Murphy use hot cell manipulators at Oak Ridge National Laboratory during the production of actinium-227.

The Department of Energy’s Oak Ridge National Laboratory is now producing actinium-227 (Ac-227) to meet projected demand for a highly effective cancer drug through a 10-year contract between the U.S. DOE Isotope Program and Bayer.

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Researchers used neutrons to probe a running engine at ORNL’s Spallation Neutron Source