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The first neutron structure of the SARS-CoV-2 main protease enzyme revealed unexpected electrical charges in the amino acids cysteine (negative) and histidine (positive), providing key data about the virus’s replication. Credit: Jill Hemman/ORNL, U.S. Dept. of Energy

To better understand how the novel coronavirus behaves and how it can be stopped, scientists have completed a three-dimensional map that reveals the location of every atom in an enzyme molecule critical to SARS-CoV-2 reproduction.

Sergei Kalinin

Five researchers at the Department of Energy’s Oak Ridge National Laboratory have been named ORNL Corporate Fellows in recognition of significant career accomplishments and continued leadership in their scientific fields.

The protease protein is both shaped like a heart and functions as one, allowing the virus replicate and spread. Inhibiting the protease would block virus reproduction. Credit: Andrey Kovalevsky/ORNL, U.S. Dept. of Energy

A team of researchers has performed the first room-temperature X-ray measurements on the SARS-CoV-2 main protease — the enzyme that enables the virus to reproduce.

A nanobrush made by pulsed laser deposition of CeO2 and Y2O3 with dim and bright bands, respectively, is seen in cross-section with scanning transmission electron microscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy

A team led by the Department of Energy’s Oak Ridge National Laboratory synthesized a tiny structure with high surface area and discovered how its unique architecture drives ions across interfaces to transport energy or information.

Smart Neighborhood homes

To better determine the potential energy cost savings among connected homes, researchers at Oak Ridge National Laboratory developed a computer simulation to more accurately compare energy use on similar weather days.

early prototype of the optical array developed by Oak Ridge National Laboratory.

IDEMIA Identity & Security USA has licensed an advanced optical array developed at Oak Ridge National Laboratory. The portable technology can be used to help identify individuals in challenging outdoor conditions.

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

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.

As part of a preliminary study, ORNL scientists used critical location data collected from Twitter to map the location of certain power outages across the United States.

Gleaning valuable data from social platforms such as Twitter—particularly to map out critical location information during emergencies— has become more effective and efficient thanks to Oak Ridge National Laboratory.