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Media Contacts
![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.
![ORNL researchers are leading virtual STEM outreach activities, such as an Internet of Things demonstration in which participants in ORCSGirls control an LED board remotely.](/sites/default/files/styles/list_page_thumbnail/public/2020-06/200411_ogi_0055_0.jpg?h=28121b77&itok=ucPjaIJO)
COVID-19 has upended nearly every aspect of our daily lives and forced us all to rethink how we can continue our work in a more physically isolated world.
![Recent research involving Oak Ridge National Laboratory’s Spallation Neutron Source demonstrates crystal-like heat conduction in a solid-liquid hybrid, AgCrSe2.](/sites/default/files/styles/list_page_thumbnail/public/2020-05/NIEDZELA_PNAS_graphic_0.png?h=39b94f55&itok=CA3sJhdS)
Research by an international team led by Duke University and the Department of Energy’s Oak Ridge National Laboratory scientists could speed the way to safer rechargeable batteries for consumer electronics such as laptops and cellphones.
![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.
![The students analyzed diatom images like this one to compare wild and genetically modified strains of these organisms. Credit: Alison Pawlicki/Oak Ridge National Laboratory, US Department of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2019-11/RI4362007.png?h=37702503&itok=9lQReLRe)
Students often participate in internships and receive formal training in their chosen career fields during college, but some pursue professional development opportunities even earlier.
![Desalination process](/sites/default/files/styles/list_page_thumbnail/public/2019-07/hydrophopicDesal04_0.jpg?h=5473d993&itok=bUBkpGOa)
A new method developed at Oak Ridge National Laboratory improves the energy efficiency of a desalination process known as solar-thermal evaporation.
![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.
![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.