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An ORNL-led team comprising researchers from multiple DOE national laboratories is using artificial intelligence and computational screening techniques – in combination with experimental validation – to identify and design five promising drug therapy approaches to target the SARS-CoV-2 virus.
Scientists at Oak Ridge National Laboratory have uncovered how the SARS-CoV-2 virus evades the human immune system by studying the interaction between a viral protein (PLpro) and a key immune protein (ISG15). These insights could guide the development of therapeutic drugs to block this interaction, enhancing the body’s ability to combat the virus.
Researchers from NASA’s Jet Propulsion Laboratory and Oak Ridge National Laboratory successfully created amorphous ice, similar to ice in interstellar space and on icy worlds in our solar system. They documented that its disordered atomic behavior is unlike any ice on Earth.
The Department of Energy’s Office of Science has selected five Oak Ridge National Laboratory scientists for Early Career Research Program awards.
From Denmark to Japan, the UK, France, and Sweden, physicist Ken Andersen has worked at neutron sources around the world. With significant contributions to neutron scattering and the scientific community, he’s now serving in his most important role yet.
When COVID-19 was declared a pandemic in March 2020, Oak Ridge National Laboratory’s Parans Paranthaman suddenly found himself working from home like millions of others.
Scientists have found new, unexpected behaviors when SARS-CoV-2 – the virus that causes COVID-19 – encounters drugs known as inhibitors, which bind to certain components of the virus and block its ability to reproduce.
Ken Andersen has been named associate laboratory director for the Neutron Sciences Directorate, or NScD, at the Department of Energy’s Oak Ridge National Laboratory.
Researchers at Oak Ridge National Laboratory’s Spallation Neutron Source have developed a diamond anvil pressure cell that will enable high-pressure science currently not possible at any other neutron source in the world.
Researchers believe that proteins could behave differently in lipid raft environments, compared to non-raft regions in a membrane, but this hypothesis has not been fully evaluated. One reason is that membrane models used to study membrane proteins rarely contain rafts.