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Carrie Wilmot

Protein in 3-D: U researcher Carrie Wilmot in front of an enlarged image of a protein structure.

Crystal clear

The world of structural biology has been better off since U professor Carrie Wilmot decided not to become a vet.

By Jack El-Hai

Jan. 3, 2007

Veterinary medicine was an early career choice for Carrie Wilmot, assistant professor in the Department of Biochemistry, Molecular Biology and Biophysics. "Then I became allergic to cats and dogs," she says.

Instead of treating animals, Wilmot transferred her interests to crystallography--the technique of determining the 3D structural arrangement of molecules by hitting crystalline samples with a beam of X-rays and studying the patterns of diffraction that result. Because of her expertise in crystallography and spectroscopy, the U.K.-native has gained wide recognition as an authority in the difficult task of successfully preparing samples of protein enzymes for analysis.

"She's world-famous for developing the techniques to catch enzymes in their different structural states as they go through the steps of their enzymatic reactions, and to trap them in a crystal so she can determine the structure," says David Thomas, who heads the structural biology group. Wilmot is one of many faculty researchers who are putting the University of Minnesota on the map and helping to transform it into one of the top three public research universities in the world within a decade.

Wilmot has focused her attention on several protein enzymes in particular. One, copper-containing amine oxidase, is implicated in such human health problems as congestive heart disease and inflammatory diseases, such as rheumatoid arthritis. When present in the blood, the enzyme can produce inflammation by drawing into surrounding tissues the cells that help fight off pathogens. The enzyme also produces formaldehyde and hydrogen peroxide, chemicals that can damage hearts already weakened by cardiac disease or diabetes. "Here is a single enzyme that represents a key step in the inflammatory response," Wilmot says.

And because the enzyme acts alone, Wilmot has found it an attractive target for investigation. Her hope is that examination of the enzyme's structure will suggest pharmaceutical approaches to inhibiting its effects. "What we're trying to do is to provide a platform of knowledge for people who want to go on and design drugs aimed at the enzyme," she says.

Also in her investigative sights are various molecular assemblies connected to Alzheimer's disease. In this research she collaborates with Karen Ashe, professor of neurology and neuroscience, who has discovered that a particular soluble form of a protein fragment is largely responsible for memory loss in Alzheimer's dementia (see "Further reading"). Ashe has succeeded in purifying this protein assembly, and Wilmot is going to solve its structure to understand why this particular form of the protein has such devastating effects in humans. "Carrie does very well researching in collaboration with other investigators," Thomas says. "Her contribution is valuable because she's [an] expert in determining protein structures."

This year the American Crystallographic Association gave Wilmot its Margaret C. Etter Early Career Award, and she earlier received the Paul D. Saltman Memorial Award from the Gordon Research Conferences.

"I'm motivated by the beauty of protein structures," she says. "I've been doing this for over a decade, but I still get such a thrill the first time I look at one. They provide the answers to so many questions, and open up so many more."

Further reading Nabbing the thief of memory.