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By Phil Williams
pwilliam@franklin.uga.edu
A team led by UGA scientist B.C. Wang is among seven groups around the nation receiving a grant under a major new initiative developed by the National Institute of General Medical Sciences, part of the National Institutes of Health.
Each of the seven groups will receive around $4 million for the first year of a five-year pilot program to study the structures of proteins in hopes of finding ways to control their actions in organisms from bacteria to plants and humans.
Wang, an internationally respected biochemist, is the lead investigator for the Southeast Collaboratory for Structural Genomics, which will analyze part of the human genome and the entire genomes of two representative organisms--the roundworm Caenorhabditis elegans and its more primitive microbial ancestor, Pyrococcus furiosus.
The team involves scientists from UGA, the University of Alabama at Birmingham and Georgia State University, as well as collaborators from the Oklahoma Medical Foundation, the University of Alabama at Huntsville, Harvard Medical School and Research Genetics, Inc.
Others from the University of Georgia involved in the project are James Prestegard, Georgia Research Alliance Eminent Scholar in nuclear magnetic resonance spectroscopy, and Fang Tian, both with UGA’s Complex Carbohydrate Research Center; Harry A. Dailey Jr., microbiology; Jonathan Arnold and R. David Hall, genetics; M. Gary Newton, chemistry; and Michael W.W. Adams, James Liu, James Omichinski and John P. Rose, biochemistry and molecular biology.
“Biomedical research is the next great frontier of knowledge and the National Institutes of Health are clearly seeking out the best researchers to address some of the most fundamental issues of human health,” says UGA President Michael F. Adams. “The University of Georgia’s participation in this major NIH grant puts us among the elite in the field of structural genomics. I would like to congratulate Dr. Wang and his associates on their success.”
Wang, who came to the university in 1995 as a Ramsey-Georgia Research Alliance Eminent Scholar, is an expert in X-ray crystallography. The Southeast Collaboratory for Structural Genomics emphasizes technology development, especially for automated crystallography and nuclear magnetic resonance techniques.
UGA Provost Karen Holbrook provided crucial support during the development of the proposal, according to Wang: “She correctly insisted that we could compete with the top research programs in the country.” Michael Cassidy, president of the Georgia Research Alliance, also has shown strong interest in the pilot program, Wang says.
Wang’s research team will develop and test experimental and computational methods for cost-effective, high-speed solutions to protein structures. They will then apply what they learn to scan the entire genome of two species: a eukaryote (an organism with one or more cells containing well-defined nuclei) and a prokaryote (an organism such as a bacterium or blue-green alga, whose nucleus lacks a limiting membrane).
The eukaryotic organism is the much-studied tiny worm called Caenorhabditis elegans, while the ancestrally related prokaryotic organism is the extreme-heat loving organism Pyrococcus furiosus, which flourishes around thermal vents in oceans or in hot springs.
“As human DNAs from the National Cancer Institute-sponsored genome project become available, they will be included in the study, with the ultimate goal being the structural characterization of all proteins in the human genome,” says Wang.
There are four work areas in the group: bioinformatics, protein production, nuclear magnetic resonance imaging and X-ray crystallography. Using newly designed robotics, the protein production team will supply approximately 80 proteins a week for both NMR and X-ray crystallography studies.
Wang says the NMR group has already developed methods that could potentially lead to high-throughput methods, and the X-ray crystallography team has come up with three different innovative approaches that will make rapid structural determination possible. They are crystallization of proteins using microgram sample quantities, an increased data-collection ability using the synchrotron equipment at Argonne National Laboratory outside Chicago, and a breakthrough in direct determination of protein structure.
“We believe study will lead to a dramatic improvement in the speed at which we can determine the structures of proteins,” says Wang. “We see this as a logical and important next step in the study of the human genome.”
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