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Media Contacts
![Computational biophysicist Ada Sedova is using experiments and high-performance computing to explore the properties of biological systems and predict their form and function, including research to accelerate drug discovery for COVID-19. Photo credit: Jason Richards, Oak Ridge National Laboratory, U.S. Dept. of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2020-07/2017-P06162Cropped.jpg?h=f1d4573a&itok=TrvR_opt)
Ada Sedova’s journey to Oak Ridge National Laboratory has taken her on the path from pre-med studies in college to an accelerated graduate career in mathematics and biophysics and now to the intersection of computational science and biology
![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.
![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.
![Matthew R. Ryder](/sites/default/files/styles/list_page_thumbnail/public/2020-06/Ryder_Headshot%5B1%5D.jpg?h=5c245560&itok=LrhlzkyS)
Matthew R. Ryder, a researcher at the Department of Energy’s Oak Ridge National Laboratory, has been named the 2020 Foresight Fellow in Molecular-Scale Engineering.
![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.
![The students analyzed diatom images like this one to compare wild and genetically modified strains of these organisms. Credit: Alison Pawlicki/Oak Ridge National Laboratory, US Department of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2019-11/RI4362007.png?h=37702503&itok=9lQReLRe)
Students often participate in internships and receive formal training in their chosen career fields during college, but some pursue professional development opportunities even earlier.
![Desalination process](/sites/default/files/styles/list_page_thumbnail/public/2019-07/hydrophopicDesal04_0.jpg?h=5473d993&itok=bUBkpGOa)
A new method developed at Oak Ridge National Laboratory improves the energy efficiency of a desalination process known as solar-thermal evaporation.
![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.