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Media Contacts
![Starch granules](/sites/default/files/styles/list_page_thumbnail/public/2020-02/starchgranules.png?h=0c9ab501&itok=eLsE3JOx)
Scientists at the Department of Energy’s Oak Ridge National Laboratory have developed a new method to peer deep into the nanostructure of biomaterials without damaging the sample. This novel technique can confirm structural features in starch, a carbohydrate important in biofuel production.
![Background image represents the cobalt oxide structure Goodenough demonstrated could produce four volts of electricity with intercalated lithium ions. This early research led to energy storage and performance advances in myriad electronic applications. Credit: Jill Hemman/Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-10/19-g01251_nobel.png?h=e4fbc3eb&itok=R0uVyKRm)
Two of the researchers who share the Nobel Prize in Chemistry announced Wednesday—John B. Goodenough of the University of Texas at Austin and M. Stanley Whittingham of Binghamton University in New York—have research ties to ORNL.
![quantum mechanics to advance a range of technologies including computing, fiber optics and network communication](/sites/default/files/styles/list_page_thumbnail/public/2019-09/2017-P08412_0.jpg?h=b6236d98&itok=ecQNon31)
Three researchers at Oak Ridge National Laboratory will lead or participate in collaborative research projects aimed at harnessing the power of quantum mechanics to advance a range of technologies including computing, fiber optics and network
![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.