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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.
![A nanobrush made by pulsed laser deposition of CeO2 and Y2O3 with dim and bright bands, respectively, is seen in cross-section with scanning transmission electron microscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-06/HAADF-137804_FIRE_scale_0.jpg?h=ea2c671e&itok=8URQqQi6)
A team led by the Department of Energy’s Oak Ridge National Laboratory synthesized a tiny structure with high surface area and discovered how its unique architecture drives ions across interfaces to transport energy or information.
![Matthew R. Ryder](/sites/default/files/styles/list_page_thumbnail/public/2020-06/Ryder_Headshot%5B1%5D.jpg?h=5c245560&itok=LrhlzkyS)
Matthew R. Ryder, a researcher at the Department of Energy’s Oak Ridge National Laboratory, has been named the 2020 Foresight Fellow in Molecular-Scale Engineering.
![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.
![Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-12/19-G01458_Cheng_PR.png?h=14829302&itok=U1YwTrlo)
Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy
![CellSight allows for rapid mass spectrometry of individual cells. Credit: John Cahill, Oak Ridge National Laboratory/U.S. Dept of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-10/4CellSightPhoto_0.png?h=67debf3e&itok=fmsxiN_b)
Researchers at the Department of Energy’s Oak Ridge National Laboratory have received five 2019 R&D 100 Awards, increasing the lab’s total to 221 since the award’s inception in 1963.
![Materials—Engineering heat transport](/sites/default/files/styles/list_page_thumbnail/public/2019-05/Materials-Engineering_heat_transport.png?h=abd215d5&itok=PJPSWa9s)
Scientists have discovered a way to alter heat transport in thermoelectric materials, a finding that may ultimately improve energy efficiency as the materials
![Snowflakes indicate phases of super-cold ice](/sites/default/files/styles/list_page_thumbnail/public/2019-05/19-G00404_Tulk_PR_0.jpg?h=e4fbc3eb&itok=5fn8aUhP)
An ORNL-led team's observation of certain crystalline ice phases challenges accepted theories about super-cooled water and non-crystalline ice. Their findings, reported in the journal Nature, will also lead to better understanding of ice and its various phases found on other planets, moons and elsewhere in space.
![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.