Lab experiments support COVID-19 bradykinin storm theory

A new paper published in Nature Communications adds further evidence to the bradykinin storm theory of COVID-19’s viral pathogenesis — a theory that was posited two years ago by a team of researchers at the Department of Energy’s Oak Ridge National Laboratory.


UT-Battelle recognized with Defense Secretary’s Freedom Award

The Department of Defense has recognized UT-Battelle with a 2022 Secretary of Defense Employer Support Freedom Award, the highest recognition given by the United States government to employers for their support of staff members who serve as reserve members of the U.S. Armed Forces, known collectively as the Reserve component.


Using fusion technology, scientists probe the depths of the earth

Researchers in the geothermal energy industry are joining forces with fusion experts at the Department of Energy’s Oak Ridge National Laboratory to repurpose gyrotron technology, a tool used in fusion. Gyrotrons produce high-powered microwaves to heat up fusion plasmas.


Fernanda Santos: Digging into charred landscapes for clues to carbon storage

With wildfires increasing in scope and intensity around the world, Fernanda Santos’ research into how such calamities affect soil carbon storage has taken on new urgency.

The Oak Ridge National Laboratory soil biogeochemist has been digging into charred landscapes to better understand what happens to belowground biodiversity after such disturbances and how that affects the soil carbon cycle.


Using math to predict SARS-CoV-2 protein mutations

Oak Ridge National Laboratory, the University of Tennessee at Chattanooga and Tuskegee University researchers used mathematics to predict which areas of the SARS-CoV-2 spike protein are most likely to mutate.

In a study supported by the National Science Foundation, the team analyzed the topology of more than 13,000 Protein Data Bank structures and found that mutations in the virus’s spike protein were most likely to occur in areas with high topological free energy, which makes a protein less stable.