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The Department of Energy’s Office of Science has selected three ORNL research teams to receive funding through DOE’s new Biopreparedness Research Virtual Environment initiative.

ORNL seismic researcher Chengping Chai placed seismic sensors on the ground at various distances from an ORNL nuclear reactor to learn whether they could detect its operating state. Credit: Carlos Jones/ORNL, U.S. Dept. of Energy

Like most scientists, Chengping Chai is not content with the surface of things: He wants to probe beyond to learn what’s really going on. But in his case, he is literally building a map of the world beneath, using seismic and acoustic data that reveal when and where the earth moves.

A pure lipid membrane formed using lipid-coated water droplets exhibits long-term potentiation, or LTP, associated with learning and memory, emulating hippocampal LTP observed in the brains of mammals and birds. Credit: Jill Hemman/ORNL, U.S. Dept. of Energy

While studying how bio-inspired materials might inform the design of next-generation computers, scientists at ORNL achieved a first-of-its-kind result that could have big implications for both edge computing and human health.

Magnetic quantum material broadens platform for probing next-gen information technologies

Scientists at ORNL used neutron scattering to determine whether a specific material’s atomic structure could host a novel state of matter called a spiral spin liquid.

Mars Rover 2020

More than 50 current employees and recent retirees from ORNL received Department of Energy Secretary’s Honor Awards from Secretary Jennifer Granholm in January as part of project teams spanning the national laboratory system. The annual awards recognized 21 teams and three individuals for service and contributions to DOE’s mission and to the benefit of the nation.

Spin chains in a quantum system undergo a collective twisting motion as the result of quasiparticles clustering together. Demonstrating this KPZ dynamics concept are pairs of neighboring spins, shown in red, pointing upward in contrast to their peers, in blue, which alternate directions. Credit: Michelle Lehman/ORNL, U.S. Dept. of Energy

Using complementary computing calculations and neutron scattering techniques, researchers from the Department of Energy’s Oak Ridge and Lawrence Berkeley national laboratories and the University of California, Berkeley, discovered the existence of an elusive type of spin dynamics in a quantum mechanical system.

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.  

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.

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.