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Media Contacts
![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.
![Starch granules](/sites/default/files/styles/list_page_thumbnail/public/2020-02/starchgranules.png?h=0c9ab501&itok=eLsE3JOx)
Scientists at the Department of Energy’s Oak Ridge National Laboratory have developed a new method to peer deep into the nanostructure of biomaterials without damaging the sample. This novel technique can confirm structural features in starch, a carbohydrate important in biofuel production.
![Scanning probe microscopes use an atom-sharp tip—only a few nanometers thick—to image materials on a nanometer length scale. The probe tip, invisible to the eye, is attached to a cantilever (pictured) that moves across material surfaces like the tone arm on a record player. Credit: Genevieve Martin/Oak Ridge National Laboratory; U.S. Dept. of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2020-01/2019-P15115.jpg?h=c6980913&itok=o69jyoNw)
Liam Collins was drawn to study physics to understand “hidden things” and honed his expertise in microscopy so that he could bring them to light.
![Catherine Schuman during Hour of Code](/sites/default/files/styles/list_page_thumbnail/public/2019-12/IMG_0136_0.jpg?h=71976bb4&itok=56CtnbAH)
ORNL computer scientist Catherine Schuman returned to her alma mater, Harriman High School, to lead Hour of Code activities and talk to students about her job as a researcher.
![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.
![early prototype of the optical array developed by Oak Ridge National Laboratory.](/sites/default/files/styles/list_page_thumbnail/public/2019-08/Optical%20array%20tech%20demo_0.jpg?h=2992f284&itok=ahZ9Umui)
IDEMIA Identity & Security USA has licensed an advanced optical array developed at Oak Ridge National Laboratory. The portable technology can be used to help identify individuals in challenging outdoor conditions.
![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
![ORNL researcher Karren More has been elected fellow of the Microscopy Society of America.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/K_More_th.jpg?h=655057a4&itok=53tPHa-r)
OAK RIDGE, Tenn., March 22, 2019 – Karren Leslie More, a researcher at the Department of Energy’s Oak Ridge National Laboratory, has been elected fellow of the Microscopy Society of America (MSA) professional organization.
![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.