Filter News
Area of Research
- (-) Neutron Science (20)
- Biological Systems (1)
- Biology and Environment (62)
- Biology and Soft Matter (1)
- Clean Energy (77)
- Climate and Environmental Systems (1)
- Computational Biology (1)
- Computational Engineering (1)
- Computer Science (1)
- Fuel Cycle Science and Technology (1)
- Fusion and Fission (9)
- Fusion Energy (1)
- Isotopes (6)
- Materials (44)
- Materials for Computing (10)
- National Security (40)
- Nuclear Science and Technology (8)
- Supercomputing (70)
News Topics
- (-) Big Data (2)
- (-) Biomedical (9)
- (-) Climate Change (1)
- (-) Coronavirus (8)
- (-) Energy Storage (4)
- (-) Frontier (1)
- (-) National Security (2)
- (-) Polymers (1)
- 3-D Printing/Advanced Manufacturing (6)
- Artificial Intelligence (5)
- Bioenergy (5)
- Biology (5)
- Biotechnology (1)
- Chemical Sciences (1)
- Clean Water (2)
- Composites (1)
- Computer Science (13)
- Cybersecurity (1)
- Decarbonization (2)
- Environment (6)
- Fossil Energy (1)
- Fusion (1)
- High-Performance Computing (2)
- Machine Learning (3)
- Materials (11)
- Materials Science (20)
- Mathematics (1)
- Microscopy (2)
- Nanotechnology (8)
- Neutron Science (73)
- Nuclear Energy (2)
- Physics (8)
- Quantum Computing (1)
- Quantum Science (5)
- Security (2)
- Space Exploration (2)
- Summit (6)
- Sustainable Energy (2)
- Transportation (3)
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.
![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.
![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.
![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.
![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.