Hank Ashbaugh is working hard to unravel the mystery of unstructured proteins in the human genome, and he's on a roll. An assistant professor of chemical and biomolecular engineering at Tulane, he has received a National Science Foundation CAREER Award and $431,000 in research funding for a five-year study.
This past fall semester, Ashbaugh also received the Tulane President's Early Career Development Award in recognition of his scientific contributions and his potential as a researcher. He is a faculty member in the School of Science and Engineering.
Ashbaugh's proposal for the National Science Foundation grant explores the 20 to 30 percent of proteins in multicellular organisms that, unlike insulin, hemoglobin, phosphatases and other well-known proteins, do not have unique three-dimensional folded structures. Scientists are just beginning to study the functions of these "unfolded" proteins, which resemble a jumble of Mardi Gras beads.
"If we think of ourselves as being more complex than an amoeba, then why do we have so much unstructured material in our genome?" Ashbaugh asks. That is one of the questions he and his team, which includes Tulane students, ask themselves as they try to understand the roles of unfolded proteins.
"It's not like there's a ticker-tape parade of unfolded proteins in a body (although it may look like it)," says Ashbaugh. "These things have a function."
One of Ashbaugh's most important hypotheses suggests that these unfolded proteins play a large part in regulating communication between DNA in the command center of the cell and the rest of the cell.
The Faculty Early Career Development (CAREER) Award is considered one of the National Science Foundation's most prestigious awards. It supports the early career-development activities of teacher-scholars who most effectively integrate research and education within the context of the mission of their organization.
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