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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