Scientists gain new insights into how protective shells form around retrovirus genomes, advancing the search for drugs that will combat them.

Scientists analyzing maize affected by southern leaf blight determine the molecular structures of so-called “death acids.”

With the help of the world's strongest MRI machine, a scientist uses a novel technique to pinpoint ground zero for a migraine.

When molecules are forced to pass through narrow holes in membranes, they must move one-by-one in single file. When this “No Passing!” rule is in effect, researchers have recently made the surprising discovery that mixing two gases can lead to faster motion of some of the molecules through the narrow holes.

Andreas Neubauer took the extended stay option during his recent trip to the MagLab. After all, you can't rush art — especially when it's mixed with science.

We celebrate one of our flagship magnets and its decade of service to science.

Ten years ago the 900 Ultra-Wide Bore magnet became available to an international user community for Nuclear Magnetic Resonance spectroscopy and Magnetic Resonance Imaging at the National High Magnetic Field Lab. Since then 69 publications have been published from this instrument spanning many disciplines and the number of publications per year continues to increase with 26 in just the past 18 months demonstrating that state of the art data continues to be collected on this superb magnet.

Dynamic nuclear polarization (DNP) coupled with solid state NMR can provide orders of magnitude enhancement to normally weak NMR signals, thereby enabling the study of inherently dilute proteins such as membrane proteins. Here we demonstrate a new approach to obtain DNP signal enhancements of membrane proteins by utilizing spin labeled lipids as the polarization agents. This strategy results in more than 2x in signal enhancements of a membrane protein when compared to standard DNP sample preparation techniques.

CrgA, a key Mycobacterium tuberculosis cell division protein that recruits five other proteins to the cell division apparatus has been structurally characterized using oriented sample and magic angle spinning solid state NMR. The protein has two transmembrane helices and an intrinsically disordered N-terminus. Binding sites have been identified for it's binding partners. Evaluating these binding sites may lead to effective drugs for either promoting and inhibiting cell division, both of which are of prime interest for the treatment of tuberculosis.

By coupling selective band excitation of metabolites with high magnetic fields, relaxation-enhanced 1H MR spectroscopy can be performed in living specimen and patients to achieve high sensitivity over very short acquisition times for the examination of cellular dysfunction. This sensitivity can be used to evaluate otherwise inaccessible metabolites or regions of the proton spectral regime and can be used to probe cell-specific environments, such as neurons versus astrocytes, that may undergo differential changes during dysregulation.

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