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Powerful NMR Magnet a Boon to Research

Summer 2011The Campus  |  Share This  |  E-mail  |  Print  | 
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Magnet-CraneOnlookers cheered on the morning of Saturday, May 7, as a shattering champagne bottle christened the delivery of a $5 million, 7.5-ton magnet to Vanderbilt. The magnet is the main part of an ultra-high field, 900-megahertz nuclear magnetic resonance (NMR) spectrometer that will help researchers solve the mysteries of cancer, Alzheimer’s disease and other disorders.

Standing 9.5 feet tall, the nearly 6-foot-wide white cylinder was gingerly lowered by crane through an opening in the roof of the Biomolecular NMR Facility—with just 4 inches of clearance.

The arrival of the magnet “is a big moment for chemistry and structural biology at Vanderbilt,” says Michael Stone, professor of chemistry and chair of the department, who uses NMR to study how DNA is damaged by mutagenic chemicals. “I think it’s going to enable us to do science that is really on the cutting edge.”

The instrument is one of 10 such devices in operation in the United States, and its application at Vanderbilt to cancer drug discovery may be unique, faculty members say. It consists of superconducting alloy wire which, when cooled by liquid helium to near absolute zero, has essentially no resistance and therefore can generate an extremely high magnetic field, Stone says.

Workers install a 7.5-ton magnet that is one of only 10 such devices operating in the United States. Below: The magnet cylinder is lowered through an opening in the roof of the Biomolecular NMR Facility.

Workers install a 7.5-ton magnet that is one of only 10 such devices operating in the United States. Below: The magnet cylinder is lowered through an opening in the roof of the Biomolecular NMR Facility.

The spectrometer’s magnetic field leads to the production of detailed 3-D images on the molecular level that can reveal the structure of large, complex molecules or of smaller, drug-like molecules binding to disease-related proteins.

“Think of an old-fashioned watch that has many tiny little pieces,” explains Charles Sanders, professor of biochemistry, who uses NMR to determine the structure of large-membrane proteins associated with human disorders such as abnormal heart rhythms.

“Trying to fix a protein that’s broken in a disease without knowing the structure is like trying to fix a watch without being able to see [inside],” he says. “You have to be able to see what it is you’re trying to fix.”

“There’s a really good chance that in 10 years, Vanderbilt’s going to be a leader in taking structural biology information … and translating it into therapeutic discoveries,” Sanders predicts. “And that’s pretty exciting.”

 

© 2014 Vanderbilt University | Photography: ANNE RAYNER

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