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ORNL's Communications team works with news media seeking information about the laboratory. Media may use the resources listed below or send questions to news@ornl.gov.

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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

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.

From left, Peter Jiang, Elijah Martin and Benjamin Sulman have been selected for Early Career Research Program awards from the Department of Energy's Office of Science. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy

The Department of Energy’s Office of Science has selected three Oak Ridge National Laboratory scientists for Early Career Research Program awards.

Scientists holding 3D printed collimators

Oak Ridge National Laboratory has licensed a novel method to 3D print components used in neutron instruments for scientific research to the ExOne Company, a leading maker of binder jet 3D printing technology.

Recent research involving Oak Ridge National Laboratory’s Spallation Neutron Source demonstrates crystal-like heat conduction in a solid-liquid hybrid, AgCrSe2.

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

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

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

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

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.

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

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.