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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.

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

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.

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.

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.

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While studying the genes in poplar trees that control callus formation, scientists at Oak Ridge National Laboratory have uncovered genetic networks at the root of tumor formation in several human cancers.

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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. 

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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.

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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.

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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

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