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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.

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.

Juergen Rapp

Juergen Rapp, a distinguished R&D staff scientist in ORNL’s Fusion Energy Division in the Nuclear Science and Engineering Directorate, has been named a fellow of the American Nuclear Society

Solid radium sulfate sits in the bottom of a flask during the recovery process. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy

Oak Ridge National Laboratory researchers have discovered a better way to separate actinium-227, a rare isotope essential for an FDA-approved cancer treatment.