A team of researchers tries to unlock the mechanism of the proteins that drive muscle movement and other essential biological functions, knowledge that could lead to better treatments for high blood pressure and heart disease.

Listen to your heart beat. Take a breath. Flex a muscle. All of these actions are the responsibility of myosin, the essential motor protein that drives muscle contraction.

"As our heart beats, as we breathe, as we walk around, we're using myosin," explains Washington State University mathematics professor Edward Pate.

Myosin control the skeletal muscles responsible for every move you make, the cardiac muscle that pumps your blood, and the smooth muscles that control blood pressure, push nutrients and waste through the intestines, and drive uterine contractions. Myosin's close relative, kinesin, carries out vital functions in non-muscle cells, shepherding chromosomes to their proper places during cell division, for example, and ferrying proteins, lipids, and other molecules from neural cell bodies to distant axons.

Scientists understand the basic outlines of how myosin and kinesin do their jobs, but certain crucial details have yet to be added to the picture. Pate and his collaborators, Roger Cooke at the University of California, San Francisco, and Todd Minehardt, a former University of Colorado, Denver, professor now in the private sector, are using a combination of experimentation and simulation on NCSA's computational systems to zero in on those details. Their work focuses primarily on myosin, but because the two proteins are so closely related, insights about the muscle cell protein can be generalized to kinesin as well.

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Access Online | posted 2-22-05

 

 

 

 

 

 

 

 

 


EPR probes docked at the nucleotide binding site. (click for full image)