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Chemists Look Beyond Genome Project

February 20, 2002

Heather Heilman
Phone: 865-5714

"Proteomics" is a word that has yet to appear in most dictionaries. Protein folding is a concept that seems bizarre to most lay people. But a group of young, up-and-coming faculty members from both the uptown and downtown campuses are focused on learning more about the mysteries of protein structure and function.

Their efforts may eventually lead to treatment for a wide range of diseases that are associated with proteins gone wrong, including Alzheimer's, cystic fibrosis and Creutzfeldt-Jakob disease. Last year, the Tulane Proteomics Initiative was awarded Wall Fund money for the purchase of instrumentation.

The developing Institute for Chemical Sciences, which will focus on building collaborative research between the chemistry, biochemistry and chemical engineering departments, was funded at the same time. Biochemists have turned to the study of proteins in the aftermath of the genome project, because each gene directs the formation of a particular protein.

Jim Karam, chair of biochemistry, is supportive of interdepartmental collaboration and the increasing focus on proteomics.

"For a number of years, the focus was on genomics, ultimately culminating in the sequencing of the human genome," Karam said. "Now we're thinking about how we are going to use the information from the genome sequence to predict the proteins that are formed, their structure, their activity, and so on."

Living bodies are basically made of proteinthey are the workhorses of the cell. Cells produce proteins as long strings of amino acids, which then fold up into complex and beautiful shapes that allow the protein to perform its function. New proteins are constantly needed. Each cell makes hundred of proteins every second.

"We're trying to understand protein folding, protein structure, and protein interaction. I think that's much trickier than sequencing the genome," said Pernilla Wittung-Stafshede. Wittung-Stafshede, assistant professor of chemistry, studies proteins that bind with metal or other small organic molecules.

Her work may eventually have implications for the treatment or prevention of diseases, such as Alzheimer's, that are related to an excess of metal ions in the cell. She's also studying structures in which several proteins fold together. Wittung-Stafshede, who is Swedish, did postdoctoral work at the California Institute of Technology.

There, she started to work with proteins and helped develop a technique to use lasers to image the folding of proteins on microsecond time scale. She arrived at Tulane three years ago, where she met a colleague from the downtown campus with similar research interests. The New Orleans Protein Folding Intergroup had its beginnings in the subsequent collaboration of Wittung-Stafshede and Sam Landry, associate professor of biochemistry.

Before long they were exchanging ideas with several other members of the biochemistry department, including William Wimley, who studies the structure of membrane proteins. A defective membrane protein is the cause of cystic fibrosis, and many drugs are targeted toward membrane proteins, since they are the receptors that can allow signaled changes in the cell.

"Membrane proteins are important. And they're abundantin fact, we think that 25 percent of all proteins are membrane proteins. But they're very difficult to work on," said Wimley.

Some membrane proteins are not stable outside of the membrane. Wimley has developed model systems that make it easier to study these proteins. Other members of the group come from the Tulane-Xavier Center for Bioenvironmental Research and the chemistry departments at Loyola University and the University of New Orleans. The group meets every other week, usually at Wittung-Stafshede's uptown home.

"It's fun to interact with a core of people who are doing similar things," she said.

Citation information:

Page accessed: Thursday, November 20, 2014
Page URL: http://tulane.edu/news/releases/archive/2002/chemists_look_beyond_genome_project.cfm

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