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![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.
![Using neutrons from the TOPAZ beamline, which is optimal for locating hydrogen atoms in materials, ORNL researchers observed a single-crystal neutron diffraction structure of the insoluble carbonate salt formed by absorption of carbon dioxide from the air.](/sites/default/files/styles/list_page_thumbnail/public/2019-02/Carbon_capture_neutrons_0.jpg?h=4137a28c&itok=ZBLNFjNc)
Researchers used neutron scattering at Oak Ridge National Laboratory’s Spallation Neutron Source to investigate the effectiveness of a novel crystallization method to capture carbon dioxide directly from the air.
![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.