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Computing—Routing out the bugs

A study led by Oak Ridge National Laboratory explored the interface between the Department of Veterans Affairs’ healthcare data system and the data itself to detect the likelihood of errors and designed an auto-surveillance tool

Materials—Engineering heat transport

Scientists have discovered a way to alter heat transport in thermoelectric materials, a finding that may ultimately improve energy efficiency as the materials

The researchers used the new model to accurately identify clusters of gene mutations (spheres), which helped them study the emergence of various genetic diseases. Image credit: Ivaylo Ivanov, Georgia State University.

Environmental conditions, lifestyle choices, chemical exposure, and foodborne and airborne pathogens are among the external factors that can cause disease. In contrast, internal genetic factors can be responsible for the onset and progression of diseases ranging from degenerative neurological disorders to some cancers.

Virtual universes

Using Summit, the world’s most powerful supercomputer housed at Oak Ridge National Laboratory, a team led by Argonne National Laboratory ran three of the largest cosmological simulations known to date.

Small modular reactor computer simulation

In a step toward advancing small modular nuclear reactor designs, scientists at Oak Ridge National Laboratory have run reactor simulations on ORNL supercomputer Summit with greater-than-expected computational efficiency.

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.

ORNL researcher Karren More has been elected fellow of the Microscopy Society of America.

OAK RIDGE, Tenn., March 22, 2019 – Karren Leslie More, a researcher at the Department of Energy’s Oak Ridge National Laboratory, has been elected fellow of the Microscopy Society of America (MSA) professional organization.

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.

ORNL-led collaboration solves a beta-decay puzzle with advanced nuclear models

OAK RIDGE, Tenn., March 11, 2019—An international collaboration including scientists at the Department of Energy’s Oak Ridge National Laboratory solved a 50-year-old puzzle that explains why beta decays of atomic nuclei 

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.