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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.

Researchers at Oak Ridge National Laboratory shed new light on elusive chemical processes at the liquid-liquid interface during solvent extraction of cobalt (dark blue). Credit: Michelle Lehman/ORNL, U.S. Dept. of Energy

Real-time measurements captured by researchers at ORNL provide missing insight into chemical separations to recover cobalt, a critical raw material used to make batteries and magnets for modern technologies.

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.

Polymer self-assembly at the liquid-liquid interface in real time

OAK RIDGE, Tenn., Feb. 27, 2020 — Researchers at Oak Ridge National Laboratory and the University of Tennessee achieved a rare look at the inner workings of polymer self-assembly at an oil-water interface to advance materials for neuromorphic computing and bio-inspired technologies.