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| September
29, 2000 |
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Stanford
Laboratory Receives $6million Grant To Decipher Protein
Structures
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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, ten-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 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 your 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.
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