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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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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

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

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.

Sergei Kalinin

Five researchers at the Department of Energy’s Oak Ridge National Laboratory have been named ORNL Corporate Fellows in recognition of significant career accomplishments and continued leadership in their scientific fields.

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

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

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.

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

Using neutrons from the TOPAZ beamline, which is optimal for locating hydrogen atoms in materials, ORNL researchers observed a single-crystal neutron diffraction structure of the insoluble carbonate salt formed by absorption of carbon dioxide from the air.

Researchers used neutron scattering at Oak Ridge National Laboratory’s Spallation Neutron Source to investigate the effectiveness of a novel crystallization method to capture carbon dioxide directly from the air.

Researchers analyzed the oxygen structure (highlighted in red) found in a perovskite’s crystal structure at room temperature, 500°C and 900°C using neutron scattering at ORNL’s Spallation Neutron Source. Analyzing how these structures impact solid oxide f

A University of South Carolina research team is investigating the oxygen reduction performance of energy conversion materials called perovskites by using neutron diffraction at Oak Ridge National Laboratory’s Spallation Neutron Source.