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Frances P. Garvan-John M. Olin Medal

February 6, 2006 | A version of this story appeared in Volume 84, Issue 6

Credit: Photo by Lisa Korpiewski, U of Massachusetts
Credit: Photo by Lisa Korpiewski, U of Massachusetts

Sponsored by the Francis P. Garvan-John M. Olin Medal Endowment

Although Lila M. Gierasch was encouraged by her parents from an early age to ask "why" and to use mathematical logic, it was really her high school science teachers who made the difference, she says. "They fostered my interest in math and science. I particularly enjoyed chemistry, but I was also attracted to biology and physics. It pleases me that my career has embraced the intersection of these three, which is essentially biophysical chemistry."

As an undergrad at Mount Holyoke, she didn't really know what field would approach the questions of biology with the tools of physics and chemistry until she took a biophysics course and realized that she wanted to go further in this area.

Understanding the basic underpinnings of biological phenomena has always been Gierasch's motivation. "It is increasingly evident that biology requires proteins to fold in a challenging environment with fidelity, or devastating consequences will ensue. Misfolding and aggregation are behind many neurodegenerative and other diseases, including Alzheimer's, Parkinson's, spongiform encephalopathies, and cystic fibrosis."

Gierasch, 57, has made many important fundamental contributions to understanding the relationship between amino acid sequence and the preferred conformations of peptides and proteins. Her work helped establish the now-common approach of using peptide fragments to examine functionally important interactions of proteins. She has explored the mechanism of recognition of a broad spectrum of protein substrates by using molecular chaperones. She has described the energy landscape for the folding of a β-barrel protein, CRABP, and determined that small changes in its sequence can lead to aggregation both in vitro and in cells. Her findings suggest that a misfolded monomeric state nucleates aggregation.

Her colleagues say that she "epitomizes distinguished service to chemistry" because she is a gifted teacher who is comfortable at every student level, she is a superbly effective organizer, and she is devoted to the advancement of women in the sciences. She is internationally recognized as an outstanding scientist.

Gierasch received an A.B. in chemistry from Mount Holyoke College, South Hadley, Mass., in 1970 and a Ph.D. in biophysics from Harvard University in 1975. She began her career at Amherst College as an assistant professor of chemistry in 1974. She moved through the ranks at the University of Delaware, the University of Texas Southwestern Medical Center at Dallas, and finally the University of Massachusetts, Amherst, where she was head of the chemistry department from 1994 to 1999, and of the biochemistry and molecular biology department from 1999 to 2005, and is now professor in both departments.

Among the many honors and awards she has received are the A. P. Sloan Fellowship, a Guggenheim Fellowship, the Vincent du Vigneaud Award for Young Investigators in Peptide Research, the Chancellor's Medal from the University of Massachusetts, and a D.Sc. honoris causa from Mount Holyoke College.

She is the author of nearly 200 papers and has been the editor or adviser for several important chemistry and biochemistry journals.

The award address will be presented before the Division of Biological Chemistry.—Janet Dodd


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