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Media Contacts
![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](/sites/default/files/styles/list_page_thumbnail/public/2023-06/2023-P03398.jpg?h=3e43625b&itok=TXK8tthh)
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.
![State and Local Economic Development Award](/sites/default/files/styles/list_page_thumbnail/public/2023-01/FLCAward3_thumbnail.png?h=d1cb525d&itok=FKj_T8JY)
A partnership of ORNL, the Tennessee Department of Economic and Community Development, the Community Reuse Organization of East Tennessee and TVA that aims to attract nuclear energy-related firms to Oak Ridge has been recognized with a state and local economic development award from the Federal Laboratory Consortium.
![Paul Langan will oversee ORNL's research directorate focused on biological and environmental systems science. Credit: ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2022-12/2019-P15617_0.jpg?h=bf9cb32e&itok=4n50VPVf)
Paul Langan will join ORNL in the spring as associate laboratory director for the Biological and Environmental Systems Science Directorate.
![Michelle Kidder received the lab’s Director’s Award for Outstanding Individual Accomplishment in Science and Technology for her decades-long work mentoring students, teachers and early-career staff. Credit: Carlos Jones/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2022-11/2018-P04785_0.png?h=7a8a8cdf&itok=hysTNqXX)
Laboratory Director Thomas Zacharia presented five Director’s Awards during Saturday night's annual Awards Night event hosted by UT-Battelle, which manages ORNL for the Department of Energy.
![MDF Exterior](/sites/default/files/styles/list_page_thumbnail/public/2022-06/2021-p07609.jpg?h=be3e4b3a&itok=YfKK7Wy2)
ORNL scientists will present new technologies available for licensing during the annual Technology Innovation Showcase. The event is 9 a.m. to 3 p.m. Thursday, June 16, at the Manufacturing Demonstration Facility at ORNL’s Hardin Valley campus.
![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](/sites/default/files/styles/list_page_thumbnail/public/2021-03/after_transprent_background-wFill.png?h=c71d0c67&itok=jGFt_Ggj)
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.
![ORNL is designing a neutronic research engine to evaluate new materials and designs for advanced vehicles using the facilities at the Spallation Neutron Source at ORNL. Credit: Jill Hemman/ORNL, U.S. Dept of Energy, and Southwest Research Institute.](/sites/default/files/styles/list_page_thumbnail/public/2020-12/20-G01771_VULCAN_engine_proof1.png?h=e4fbc3eb&itok=f6owlGkE)
In the quest for advanced vehicles with higher energy efficiency and ultra-low emissions, ORNL researchers are accelerating a research engine that gives scientists and engineers an unprecedented view inside the atomic-level workings of combustion engines in real time.
![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](/sites/default/files/styles/list_page_thumbnail/public/2020-10/20-G01620_Protease_PR_proof2_0.jpg?h=3e3883a3&itok=XB_ZEDFQ)
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.
![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](/sites/default/files/styles/list_page_thumbnail/public/2020-07/THF_high_res.gif?h=5a472534&itok=5peedFnF)
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](/sites/default/files/styles/list_page_thumbnail/public/2020-06/protease_dimer_3_1.png?h=aa51a450&itok=sJY7AB8d)
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.