October 9, 2007
Mary Ann Travis
Why is disorder the state of a quarter of the proteins in our bodies? asks Henry Ashbaugh. By asking questions like this about expanded and unstructured proteins and exploring answers through thermodynamics, Ashbaugh has received the Tulane President’s Early Career Development Award.
Ashbaugh, assistant professor of chemical and biomolecular engineering, was chosen for the award because of his potential as a researcher and because he has already made significant contributions to the study of “natively unfolded proteins” and how they interact with each other.
Ashbaugh is the fourth recipient of the Early Career Development Award. Nominations for the award are made by departmental chairs and must be supported by a dean — in Ashbaugh’s case, Nick Altiero, dean of the School of Science and Engineering. Tulane President Scott Cowen makes the final selection.
The standard picture of proteins is that they fold into unique, three-dimensional structures. Proteins do molecular “origami” inside the cell and fold into shapes called their native structure. Folded proteins function as enzymes, hormones and regulators in cells.
But scientists have learned in the past decade that 20 to 30 percent of the proteins in complex cells have no structure. So Ashbaugh asks, “How is disorder helping us be able to accomplish what we need to do?”
Because complex cells have so many unfolded proteins, they must be doing something, says Ashbaugh. He and his team are trying to understand the roles unfolded proteins may play in regulating communication back and forth between the command center of the cell and the rest of the cell.
Unfolded proteins are ropelike, and they form a tangled web in the “nuclear pore complex,” which is essentially the gate between the cell nucleus and the cytoplasm.
Ashbaugh’s team of collaborators includes graduate and undergraduate students as well as colleagues at Tulane and other universities and research institutions. His research interests also lie in polymers and aqueous solutions. “That’s life,” he says, “because we’re basically big sacks of water.”
He is collaborating with other Tulane chemical and biomolecular engineering faculty members including professor and chair Vijay John on hydrogen storage in different phases of water and professor and associate provost Brian Mitchell on suspension of quantum dots in solutions for medical application.
With assistant professor of chemistry Scott Grayson, Ashbaugh has created a one-hour service-learning course — “Chemistry and Engineering Science in the Community.” The course fulfills the second part of the public-service graduation requirement for undergraduates, who give demonstrations of everyday uses of the scientific method to high school students.
Ashbaugh also is mentoring Harold Wick Hatch, a Tulane senior, who was awarded a Goldwater scholarship this year. Hatch took Ashbaugh’s “Introduction to Thermodynamics” when he was a sophomore, and they have worked together ever since on molecular simulations.
Teaching is a fun aspect of being a faculty member, says Ashbaugh, who adds that post-Katrina is an interesting time to be at Tulane.
His mathematical approach to thermodynamics sometimes shocks students who must begin to synthesize things they’ve learned in other classes and think critically.
“I think to hit students what you need is to show them that you care,” he adds. “And that you’re willing to do what it takes to get them there -- not to show them that you know it better than they do.”
The teaching balances the research, Ashbaugh says. And vice versa. “The research drives the inspiration for being here in an academic environment.”
By letting students in on his research, Ashbaugh shows them where a subject like thermodynamics can go if they stay with it. And then, perhaps, they, too, can find meaning in disorder.
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