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Media Contacts
![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.
![Colorized micrograph of lily pollen](/sites/default/files/styles/list_page_thumbnail/public/2020-07/Lily_CH%20and%20CO_1.png?h=436b82d4&itok=lntoWKVr)
Oak Ridge National Laboratory researchers have built a novel microscope that provides a “chemical lens” for viewing biological systems including cell membranes and biofilms.
![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.
![Materials — Molding molecular matter](/sites/default/files/styles/list_page_thumbnail/public/2020-04/Ebeam_IMAGE_Final_0.jpg?h=c4322a57&itok=uYF8ugqx)
Scientists at Oak Ridge National Laboratory used a focused beam of electrons to stitch platinum-silicon molecules into graphene, marking the first deliberate insertion of artificial molecules into a graphene host matrix.
![CellSight allows for rapid mass spectrometry of individual cells. Credit: John Cahill, Oak Ridge National Laboratory/U.S. Dept of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-10/4CellSightPhoto_0.png?h=67debf3e&itok=fmsxiN_b)
Researchers at the Department of Energy’s Oak Ridge National Laboratory have received five 2019 R&D 100 Awards, increasing the lab’s total to 221 since the award’s inception in 1963.
![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
![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.
![ORNL alanine_graphic.jpg ORNL alanine_graphic.jpg](/sites/default/files/styles/list_page_thumbnail/public/ORNL%20alanine_graphic.jpg?itok=iRLfcOw-)
OAK RIDGE, Tenn., Jan. 31, 2019—A new electron microscopy technique that detects the subtle changes in the weight of proteins at the nanoscale—while keeping the sample intact—could open a new pathway for deeper, more comprehensive studies of the basic building blocks of life.
![Picture2.png Picture2.png](/sites/default/files/styles/list_page_thumbnail/public/Picture2_1.png?itok=IV4n9XEh)
Oak Ridge National Laboratory scientists studying fuel cells as a potential alternative to internal combustion engines used sophisticated electron microscopy to investigate the benefits of replacing high-cost platinum with a lower cost, carbon-nitrogen-manganese-based catalyst.