The effects of a stomach flu can range from pesky to deadly. Researchers recently used an AI program to predict the structure of a common rotavirus and collaborated with a Biosciences researcher working at the Advanced Light Source to validate their novel finding.
Study Expands Horizons for DNA Nanotechnology
Researchers at Arizona State University’s Biodesign Institute conducted the first systematic study of Holliday junctions—the nexus of two segments of double-stranded DNA—using crystallography techniques performed at the Advanced Light Source, the Argonne Photon Source, and the National Synchrotron Light Source II.
Enzyme Structure Reveals Key Details in Strigolactone Signaling
A recent study published in Nature Plants used a combination of genetic mutation and X-ray crystallography, conducted at the Berkeley Center for Structural Biology, to reveal structural details of a key enzyme involved in plant signaling.
DNA Synthesis: Flip It and Reverse It
Every time our cells divide, the DNA inside must be copied accurately to avoid mistakes that could be harmful to our health. Known as DNA synthesis, the precise sequence of steps has until now only been hypothesized. In a recent study, timestamps have been added to step-by-step snapshots, revealing a switch-up between two of the steps that, if replicated in additional studies, would upend our current assumptions of the process.
BCSB Determines Interactions of Potential Inhibitor with SARS-CoV-2 Protease
Researchers from the Baylor College of Medicine employed previously constructed DNA-encoded chemistry technology (DEC-tec) libraries to identify several candidate molecules that could inhibit the action of Mpro, the main protease of SARS-CoV-2. In a recent study, the researchers described CDD-1713, a new inhibitor to the enzyme Mpro that is involved in propagating the virus. The X-ray crystallographic data, which was collected by Banumathi Sankaran in the Molecular Biophysics and Integrated Bioimaging Division, allowed the researchers to determine that CDD-1713 inhibits the activity of Mpro by binding in the active site of this enzyme.
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