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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.
![To develop complex materials with superior properties, Vera Bocharova uses diverse methods including broadband dielectric spectroscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy; photographer Jason Richards](/sites/default/files/styles/list_page_thumbnail/public/2019-02/2016-p05202.jpg?h=b6236d98&itok=w-Sd8giq)
Vera Bocharova at the Department of Energy’s Oak Ridge National Laboratory investigates the structure and dynamics of soft materials—polymer nanocomposites, polymer electrolytes and biological macromolecules—to advance materials and technologies for energy, medicine and other applications.
![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.
![2018-P07635 BL-6 user - Univ of Guelph-6004R_sm[2].jpg 2018-P07635 BL-6 user - Univ of Guelph-6004R_sm[2].jpg](/sites/default/files/styles/list_page_thumbnail/public/2018-P07635%20BL-6%20user%20-%20Univ%20of%20Guelph-6004R_sm%5B2%5D.jpg?itok=DUdZNt_q)
A team of scientists, led by University of Guelph professor John Dutcher, are using neutrons at ORNL’s Spallation Neutron Source to unlock the secrets of natural nanoparticles that could be used to improve medicines.
![Physics_silicon-detectors.jpg](/sites/default/files/styles/list_page_thumbnail/public/Physics_silicon-detectors.jpg?h=c920d705&itok=Q1fP5ZTi)
Physicists turned to the “doubly magic” tin isotope Sn-132, colliding it with a target at Oak Ridge National Laboratory to assess its properties as it lost a neutron to become Sn-131.
![Two neutron diffraction experiments (represented by pink and blue neutron beams) probed a salty solution to reveal its atomic structure. The only difference between the experiments was the identity of the oxygen isotope (O*) that labeled nitrate molecules Two neutron diffraction experiments (represented by pink and blue neutron beams) probed a salty solution to reveal its atomic structure. The only difference between the experiments was the identity of the oxygen isotope (O*) that labeled nitrate molecules](/sites/default/files/styles/list_page_thumbnail/public/news/images/ORNL%202018-G01254-AM-01.jpg?itok=WXkmqIs1)
Scientists at the Department of Energy’s Oak Ridge National Laboratory used neutrons, isotopes and simulations to “see” the atomic structure of a saturated solution and found evidence supporting one of two competing hypotheses about how ions come
![B_Hudak_ORNL.jpg B_Hudak_ORNL.jpg](/sites/default/files/styles/list_page_thumbnail/public/B_Hudak_ORNL.jpg?itok=Os5uKm-q)
An Oak Ridge National Laboratory-led team used a scanning transmission electron microscope to selectively position single atoms below a crystal’s surface for the first time.
![Sergei Kalinin, director of the Institute for Functional Imaging of Materials at Oak Ridge National Laboratory, convenes experts in microscopy and computing to gain scientific insights that will inform design of advanced materials for energy and informati Sergei Kalinin, director of the Institute for Functional Imaging of Materials at Oak Ridge National Laboratory, convenes experts in microscopy and computing to gain scientific insights that will inform design of advanced materials for energy and informati](/sites/default/files/styles/list_page_thumbnail/public/news/images/2018-P00854%20%28002%29.jpg?itok=UfhMWf3G)
Sergei Kalinin of the Department of Energy’s Oak Ridge National Laboratory knows that seeing something is not the same as understanding it. As director of ORNL’s Institute for Functional Imaging of Materials, he convenes experts in microscopy and computing to gain scientific insigh...