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Stanford Synchrotron Radiation Laboratory receives $6 million grant to decipher protein structures
Now that a map of the human genome is nearly complete, scientists face a new challenge -- understanding the form and function of the proteins our genes produce.
As part of a nationwide research effort, the Stanford Synchrotron Radiation Laboratory (SSRL) has been awarded a five-year grant to participate in determining the three-dimensional structure of 2,000 proteins encoded by human DNA.
The grant is part of a new, 10-year initiative launched by the National Institute of General Medical Sciences (NIGMS) -- part of the National Institutes of Health that funds a significant amount of basic biomedical science.
On Sept. 26, NIGMS awarded nearly $150 million to seven projects around the country, including $24 million to the Joint Center for Structural Genomics (JCSG) -- a consortium of California scientific research organizations that includes SSRL, the Scripps Research Institute and the University of California-San Diego.
The goal of the consortium is to develop high-throughput methods for protein production, crystallization and structure determination.
Beginning Oct. 1, SSRL will receive about $6 million over 5 years from JCSG to establish a structure determination center for the consortium.
Using the Stanford synchrotron's powerful X-ray crystallography instruments, SSRL researchers will obtain detailed, 3-D images of human and animal proteins at the molecular level with heretofore unprecedented speed.
"Synchrotron radiation research provides major opportunities for understanding the structure and functional relationships of genes," says Jonathan Dorfan, director of the Stanford Linear Accelerator Center that oversees SSRL.
"SSRL has a well established and growing program which underpins the new development plans," he adds, and one that "leverages upon the significant investment of the Department of Energy which funds the operations of SSRL."
All organisms -- from bacteria to plants to people -- need proteins to survive. Some defend against disease, while others regulate body functions. Specialized proteins called enzymes drive chemical reactions in the cell, while structural proteins combine to form cartilage, fingernails and hair.
It turns out that nearly every molecule of protein produced in the body has to be folded into a specific, three-dimensional shape in order to function properly. Humans produce thousands of proteins, each with a distinct function and shape. Some resemble convoluted pretzels, while others are woven into intricate braids.
X-ray crytallography images of the protein hemoglobin, for example, reveal a complex molecule resembling a ball of twisted ribbon -- a unique shape that allows hemoglobin to carry oxygen through the bloodstream. If the molecule is folded incorrectly, oxygen will not be delivered.
According to JCSG, detailed, three-dimensional images of proteins will give researchers a clearer picture of how protein structure and function are interrelated.
"Structural genomics will allow researchers from the life, physical and medical sciences to gain a deeper understanding of basic life processes, evolution and disease," comments SSRL Professor Peter Kuhn.
"Synchrotron-based macromolecular crystallography has revolutionized our ability to determine structures with much higher quality and at a much faster rate than ever before possible," adds Keith Hodgson, SSRL director and Stanford professor of chemistry.
"New developments in robotics and software at JCSG will be a central component in achieving our goals," he concludes.
By Mark Shwartz