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Media Contacts
![An organic solvent and water separate and form nanoclusters on the hydrophobic and hydrophilic sections of plant material, driving the efficient deconstruction of biomass. Credit: Michelle Lehman/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-11/dark_image_small.png?h=2e111cc1&itok=drKqW05b)
Experiments led by researchers at ORNL have determined that several hepatitis C drugs can inhibit the SARS-CoV-2 main protease, a crucial protein enzyme that enables the novel coronavirus to reproduce.
![The first neutron structure of the SARS-CoV-2 main protease enzyme revealed unexpected electrical charges in the amino acids cysteine (negative) and histidine (positive), providing key data about the virus’s replication. Credit: Jill Hemman/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-10/20-G01620_Protease_PR_proof2_0.jpg?h=3e3883a3&itok=XB_ZEDFQ)
To better understand how the novel coronavirus behaves and how it can be stopped, scientists have completed a three-dimensional map that reveals the location of every atom in an enzyme molecule critical to SARS-CoV-2 reproduction.
![Analyses of lung fluid cells from COVID-19 patients conducted on the nation’s fastest supercomputer point to gene expression patterns that may explain the runaway symptoms produced by the body’s response to SARS-CoV-2. Credit: Jason B. Smith/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-07/cells%20200%5B1%5D.png?h=b95f6d72&itok=V2OxqL5l)
A team led by Dan Jacobson of Oak Ridge National Laboratory used the Summit supercomputer at ORNL to analyze genes from cells in the lung fluid of nine COVID-19 patients compared with 40 control patients.
![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.
![Before the demonstration, the team prepared QKD equipment (pictured) at ORNL. Image credit: Genevieve Martin/Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-05/2020-P01652_0.jpg?h=c6980913&itok=qHZPZfd6)
For the second year in a row, a team from the Department of Energy’s Oak Ridge and Los Alamos national laboratories led a demonstration hosted by EPB, a community-based utility and telecommunications company serving Chattanooga, Tennessee.
![Transformational Challenge Reactor Demonstration items](/sites/default/files/styles/list_page_thumbnail/public/2020-03/Press_release_image.jpg?h=b707efd5&itok=-Sxbmt8D)
Researchers at the Department of Energy’s Oak Ridge National Laboratory are refining their design of a 3D-printed nuclear reactor core, scaling up the additive manufacturing process necessary to build it, and developing methods
![Summit supercomputer](/sites/default/files/styles/list_page_thumbnail/public/2019-09/42957291821_d77b1c6051_o_0.jpg?h=b241dec4&itok=K_s_UmII)
Processes like manufacturing aircraft parts, analyzing data from doctors’ notes and identifying national security threats may seem unrelated, but at the U.S. Department of Energy’s Oak Ridge National Laboratory, artificial intelligence is improving all of these tasks.
![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.
![(From left) ORNL Associate Laboratory Director for Computing and Computational Sciences Jeff Nichols; ORNL Health Data Sciences Institute Director Gina Tourassi; DOE Deputy Under Secretary for Science Thomas Cubbage; ORNL Task Lead for Biostatistics Blair Christian; and ORNL Research Scientist Ioana Danciu were invited to the White House to showcase an ORNL-developed digital tool aimed at better matching cancer patients with clinical trials.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/TourassiWH%5B1%5D.png?h=26b5064d&itok=HUC2iYmE)
OAK RIDGE, Tenn., March 4, 2019—A team of researchers from the Department of Energy’s Oak Ridge National Laboratory Health Data Sciences Institute have harnessed the power of artificial intelligence to better match cancer patients with clinical trials.
OAK RIDGE, Tenn., Feb. 12, 2019—A team of researchers from the Department of Energy’s Oak Ridge and Los Alamos National Laboratories has partnered with EPB, a Chattanooga utility and telecommunications company, to demonstrate the effectiveness of metro-scale quantum key distribution (QKD).