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Media Contacts
![ORNL collaborator Hsiu-Wen Wang led the neutron scattering experiments at the Spallation Neutron Source to probe complex electrolyte solutions that challenge nuclear waste processing at Hanford and other sites. Credit: Genevieve Martin/Oak Ridge National Laboratory, U.S. Dept. of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2019-05/2019-P01240_0.jpg?h=c6980913&itok=RLLi1M-g)
Researchers at the Department of Energy’s Oak Ridge National Laboratory, Pacific Northwest National Laboratory and Washington State University teamed up to investigate the complex dynamics of low-water liquids that challenge nuclear waste processing at federal cleanup sites.
![The illustrations show how the correlation between lattice distortion and proton binding energy in a material affects proton conduction in different environments. Mitigating this interaction could help researchers improve the ionic conductivity of solid materials.](/sites/default/files/styles/list_page_thumbnail/public/2019-05/Figure_Rosenthal_5-1-19_0.png?h=73c01546&itok=-tjVhDfm)
Ionic conduction involves the movement of ions from one location to another inside a material. The ions travel through point defects, which are irregularities in the otherwise consistent arrangement of atoms known as the crystal lattice. This sometimes sluggish process can limit the performance and efficiency of fuel cells, batteries, and other energy storage technologies.
![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](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
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.