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Oak Ridge National Laboratory’s Leah Broussard shows a neutron-absorbing "wall" that stops all neutrons but in theory would allow hypothetical mirror neutrons to pass through. Credit: Genevieve Martin/ORNL, U.S. Dept. of Energy

To solve a long-standing puzzle about how long a neutron can “live” outside an atomic nucleus, physicists entertained a wild but testable theory positing the existence of a right-handed version of our left-handed universe.

Three ORNL scientists have been elected fellows of the American Association for the Advancement of Science, or AAAS, the world’s largest general scientific society and publisher of the Science family of journals. Credit: ORNL, U.S. Dept. of Energy

Three ORNL scientists have been elected fellows of the American Association for the Advancement of Science, or AAAS, the world’s largest general scientific society and publisher of the Science family of journals.

Neutron scattering experiments show electric charges, shown in red, blue and grey, in the SARS-CoV-2 main protease site where telaprevir binds to the structure. The experiments provide critical data for the design of small-molecule drugs to treat COVID-19. Credit: Jill Hemman and Michelle Lehman/ORNL, U.S. Dept. of Energy

Scientists have found new, unexpected behaviors when SARS-CoV-2 – the virus that causes COVID-19 – encounters drugs known as inhibitors, which bind to certain components of the virus and block its ability to reproduce.  

SCGSR Awardee Jacob Zettlemoyer, Indiana University Bloomington, led data analysis and worked with ORNL’s Mike Febbraro on coatings, shown under blue light, to shift argon light to visible wavelengths to boost detection. Credit: Rex Tayloe/Indiana University

The COHERENT particle physics experiment at the Department of Energy’s Oak Ridge National Laboratory has firmly established the existence of a new kind of neutrino interaction.

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.

Oak Ridge National Laboratory entrance sign

Geoffrey L. Greene, a professor at the University of Tennessee, Knoxville, who holds a joint appointment with ORNL, will be awarded the 2021 Tom Bonner Prize for Nuclear Physics from the American Physical Society.

The n-helium-3 precision experiment, conducted at ORNL, measured the weak force between protons and neutrons by detecting the tiny electrical signal produced when a neutron and a helium-3 nucleus combine and then decay as they move through the helium gas target cell. Credit: Andy Sproles/ORNL, U.S. Dept. of Energy

Through a one-of-a-kind experiment at ORNL, nuclear physicists have precisely measured the weak interaction between protons and neutrons. The result quantifies the weak force theory as predicted by the Standard Model of Particle Physics.

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.

Snowflakes indicate phases of super-cold ice

An ORNL-led team's observation of certain crystalline ice phases challenges accepted theories about super-cooled water and non-crystalline ice. Their findings, reported in the journal Nature, will also lead to better understanding of ice and its various phases found on other planets, moons and elsewhere in space.

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.