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Media Contacts
![Enzyme activity during organophosphate poisoning](/sites/default/files/styles/list_page_thumbnail/public/2020-08/anecdote1_0.png?h=d1cb525d&itok=wpYYilBI)
Pick your poison. It can be deadly for good reasons such as protecting crops from harmful insects or fighting parasite infection as medicine — or for evil as a weapon for bioterrorism. Or, in extremely diluted amounts, it can be used to enhance beauty.
![Sergei Kalinin](/sites/default/files/styles/list_page_thumbnail/public/2020-07/2019-P00126_0.png?h=5969a3b5&itok=66cucDCt)
Five researchers at the Department of Energy’s Oak Ridge National Laboratory have been named ORNL Corporate Fellows in recognition of significant career accomplishments and continued leadership in their scientific fields.
![The protease protein is both shaped like a heart and functions as one, allowing the virus replicate and spread. Inhibiting the protease would block virus reproduction. Credit: Andrey Kovalevsky/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-06/protease_dimer_3_1.png?h=aa51a450&itok=sJY7AB8d)
A team of researchers has performed the first room-temperature X-ray measurements on the SARS-CoV-2 main protease — the enzyme that enables the virus to reproduce.
![Coronavirus graphic](/sites/default/files/styles/list_page_thumbnail/public/2020-04/covid19_jh_0.png?h=d1cb525d&itok=PyngFUZw)
In the race to identify solutions to the COVID-19 pandemic, researchers at the Department of Energy’s Oak Ridge National Laboratory are joining the fight by applying expertise in computational science, advanced manufacturing, data science and neutron science.
![Scientists created a novel polymer that is as effective as natural proteins in transporting protons through a membrane. Credit: ORNL/Jill Hemman](/sites/default/files/styles/list_page_thumbnail/public/2020-03/19-G01195_nature_feature_0.png?h=e4fbc3eb&itok=K8czXmTr)
Biological membranes, such as the “walls” of most types of living cells, primarily consist of a double layer of lipids, or “lipid bilayer,” that forms the structure, and a variety of embedded and attached proteins with highly specialized functions, including proteins that rapidly and selectively transport ions and molecules in and out of the cell.
![Catherine Schuman during Hour of Code](/sites/default/files/styles/list_page_thumbnail/public/2019-12/IMG_0136_0.jpg?h=71976bb4&itok=56CtnbAH)
ORNL computer scientist Catherine Schuman returned to her alma mater, Harriman High School, to lead Hour of Code activities and talk to students about her job as a researcher.
![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.
![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.
![Neutron scattering allowed direct observation of how aurein induces lateral segregation in the bacteria membranes, which creates instability in the membrane structure. This instability causes the membranes to fail, making harmful bacteria less effective.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/Neutrons-FightingSuperbugs_0.jpg?h=e4b73f5a&itok=ebOQD-Mr)
As the rise of antibiotic-resistant bacteria known as superbugs threatens public health, Oak Ridge National Laboratory’s Shuo Qian and Veerendra Sharma from the Bhaba Atomic Research Centre in India are using neutron scattering to study how an antibacterial peptide interacts with and fights harmful bacteria.