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Media Contacts
![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/2020-11/dark_image_small.png?h=2e111cc1&itok=drKqW05b)
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](/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.
![Sergei Kalinin](/sites/default/files/styles/list_page_thumbnail/public/2020-07/2019-P00126_0.png?h=5969a3b5&itok=66cucDCt)
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](/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.
![ORNL’s Bianca Haberl and Amy Elliott hold 3D-printed collimators — an invention that has been licensed to ExOne, a leading binder jet 3D printer company. Credit: Genevieve Martin/Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2021-02/Amy%20and%20Bianca_Small.jpg?h=c6980913&itok=hhxhYFhi)
Oak Ridge National Laboratory has licensed a novel method to 3D print components used in neutron instruments for scientific research to the ExOne Company, a leading maker of binder jet 3D printing technology.
![A nanobrush made by pulsed laser deposition of CeO2 and Y2O3 with dim and bright bands, respectively, is seen in cross-section with scanning transmission electron microscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-06/HAADF-137804_FIRE_scale_0.jpg?h=ea2c671e&itok=8URQqQi6)
A team led by the Department of Energy’s Oak Ridge National Laboratory synthesized a tiny structure with high surface area and discovered how its unique architecture drives ions across interfaces to transport energy or information.
![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](/sites/default/files/styles/list_page_thumbnail/public/2019-11/19-G00550_MOF_PR.png?h=e4fbc3eb&itok=3cY5NUpo)
An international team of scientists, led by the University of Manchester, has developed a metal-organic framework, or MOF, material
![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](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
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.
![Neutron scattering allowed direct observation of how aurein induces lateral segregation in the bacteria membranes, which creates instability in the membrane structure. This instability causes the membranes to fail, making harmful bacteria less effective.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/Neutrons-FightingSuperbugs_0.jpg?h=e4b73f5a&itok=ebOQD-Mr)
As the rise of antibiotic-resistant bacteria known as superbugs threatens public health, Oak Ridge National Laboratory’s Shuo Qian and Veerendra Sharma from the Bhaba Atomic Research Centre in India are using neutron scattering to study how an antibacterial peptide interacts with and fights harmful bacteria.