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![Molecular dynamics simulations of the Fs-peptide revealed the presence of at least eight distinct intermediate stages during the process of protein folding. The image depicts a fully folded helix (1), various transitional forms (2–8), and one misfolded state (9). By studying these protein folding pathways, scientists hope to identify underlying factors that affect human health.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/Slide1_0.png?h=c855054e&itok=aNbgxXsc)
Using artificial neural networks designed to emulate the inner workings of the human brain, deep-learning algorithms deftly peruse and analyze large quantities of data. Applying this technique to science problems can help unearth historically elusive solutions.
![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.
![(From left) ORNL Associate Laboratory Director for Computing and Computational Sciences Jeff Nichols; ORNL Health Data Sciences Institute Director Gina Tourassi; DOE Deputy Under Secretary for Science Thomas Cubbage; ORNL Task Lead for Biostatistics Blair Christian; and ORNL Research Scientist Ioana Danciu were invited to the White House to showcase an ORNL-developed digital tool aimed at better matching cancer patients with clinical trials.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/TourassiWH%5B1%5D.png?h=26b5064d&itok=HUC2iYmE)
OAK RIDGE, Tenn., March 4, 2019—A team of researchers from the Department of Energy’s Oak Ridge National Laboratory Health Data Sciences Institute have harnessed the power of artificial intelligence to better match cancer patients with clinical trials.
![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.