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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/2020-07/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.
![Coronavirus graphic](/sites/default/files/styles/list_page_thumbnail/public/2020-04/covid19_jh_0.png?h=d1cb525d&itok=PyngFUZw)
In the race to identify solutions to the COVID-19 pandemic, researchers at the Department of Energy’s Oak Ridge National Laboratory are joining the fight by applying expertise in computational science, advanced manufacturing, data science and neutron science.
![Scientists created a novel polymer that is as effective as natural proteins in transporting protons through a membrane. Credit: ORNL/Jill Hemman](/sites/default/files/styles/list_page_thumbnail/public/2020-03/19-G01195_nature_feature_0.png?h=e4fbc3eb&itok=K8czXmTr)
Biological membranes, such as the “walls” of most types of living cells, primarily consist of a double layer of lipids, or “lipid bilayer,” that forms the structure, and a variety of embedded and attached proteins with highly specialized functions, including proteins that rapidly and selectively transport ions and molecules in and out of the cell.
![Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-12/19-G01458_Cheng_PR.png?h=14829302&itok=U1YwTrlo)
Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy
![Materials—Engineering heat transport](/sites/default/files/styles/list_page_thumbnail/public/2019-05/Materials-Engineering_heat_transport.png?h=abd215d5&itok=PJPSWa9s)
Scientists have discovered a way to alter heat transport in thermoelectric materials, a finding that may ultimately improve energy efficiency as the materials
![Snowflakes indicate phases of super-cold ice](/sites/default/files/styles/list_page_thumbnail/public/2019-05/19-G00404_Tulk_PR_0.jpg?h=e4fbc3eb&itok=5fn8aUhP)
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](/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.