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Media Contacts
![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.
![As part of a preliminary study, ORNL scientists used critical location data collected from Twitter to map the location of certain power outages across the United States.](/sites/default/files/styles/list_page_thumbnail/public/2019-02/PowerOutageTweets_map_0.png?h=6448fdc1&itok=AUit-O2Y)
Gleaning valuable data from social platforms such as Twitter—particularly to map out critical location information during emergencies— has become more effective and efficient thanks to Oak Ridge National Laboratory.
![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.
![18-G01703 PinchPoint-v2.jpg 18-G01703 PinchPoint-v2.jpg](/sites/default/files/styles/list_page_thumbnail/public/18-G01703%20PinchPoint-v2.jpg?itok=paJUPDI1)
Researchers used neutron scattering at Oak Ridge National Laboratory’s Spallation Neutron Source to investigate bizarre magnetic behavior, believed to be a possible quantum spin liquid rarely found in a three-dimensional material. QSLs are exotic states of matter where magnetism continues to fluctuate at low temperatures instead of “freezing” into aligned north and south poles as with traditional magnets.