Filter News
Area of Research
- (-) Neutron Science (10)
- (-) Nuclear Science and Technology (1)
- Advanced Manufacturing (1)
- Biological Systems (1)
- Biology and Environment (10)
- Clean Energy (28)
- Climate and Environmental Systems (1)
- Computer Science (1)
- Isotopes (1)
- Materials (13)
- Materials for Computing (1)
- National Security (3)
- Quantum information Science (1)
- Supercomputing (16)
News Topics
- (-) Biomedical (7)
- (-) Environment (4)
- 3-D Printing/Advanced Manufacturing (7)
- Advanced Reactors (6)
- Artificial Intelligence (1)
- Big Data (1)
- Bioenergy (6)
- Clean Water (1)
- Climate Change (1)
- Composites (1)
- Computer Science (10)
- Coronavirus (6)
- Decarbonization (1)
- Energy Storage (2)
- Fusion (6)
- Isotopes (4)
- Machine Learning (2)
- Materials Science (10)
- Mathematics (1)
- Microscopy (1)
- Molten Salt (1)
- Nanotechnology (4)
- National Security (1)
- Neutron Science (32)
- Nuclear Energy (20)
- Physics (5)
- Polymers (1)
- Quantum Science (2)
- Security (1)
- Space Exploration (2)
- Summit (5)
- Sustainable Energy (2)
- Transformational Challenge Reactor (3)
- Transportation (2)
Media Contacts
![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.
![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/2020-07/THF_high_res.gif?h=5a472534&itok=5peedFnF)
Scientists at ORNL used neutron scattering and supercomputing to better understand how an organic solvent and water work together to break down plant biomass, creating a pathway to significantly improve the production of renewable
![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.
![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
![Illustration of a nitrogen dioxide molecule (depicted in blue and purple) captured in a nano-size pore of an MFM-520 metal-organic framework material as observed using neutron vibrational spectroscopy at Oak Ridge National Laboratory. Image credit: ORNL/Jill Hemman](/sites/default/files/styles/list_page_thumbnail/public/2019-11/19-G00550_MOF_PR.png?h=e4fbc3eb&itok=3cY5NUpo)
An international team of scientists, led by the University of Manchester, has developed a metal-organic framework, or MOF, material
![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.