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Rutgers-Newark researcher discovers new motor protein mechanism linked to heart disease and strokes

Cardiomyopathy is an insidious disease which often strikes without warning and can lead to heart failure and eventual death. Although the disease can be traced to conditions such as high blood pressure, heart valve or arterial diseases and congenital heart defects, it is also caused by viral infections in the bloodstream. In a paper to be published in the July issue of the journal Nature Structural and Molecular Biology, a Rutgers-Newark researcher and his coworkers reveal that they have identified a possible mechanism used by an important motor protein which acts as a catalyst that enables bacteria outside the human body to travel through the blood stream and infect organs such as the heart.

The findings were published by Rutgers-Newark Chemistry Assistant Professor Charalampos Kalodimos and his coworkers, in the article, "Disorder-order folding transitions underlie catalysis in the helicase motor of SecA." Identifying the way this motor protein works is significant because it may lead to the development of new pharmacological therapies which can target and kill the bacteria to prevent or minimize damage to the heart muscle. The results follow nearly two years of research funded by a $300,000 American Heart Association (AHA) grant. The AHA agreed to support Kalodimos's research because he is focusing on specific bacteria that cause cardiovascular diseases in both adults and children.

Using high-resolution NMR Spectroscopy technology, Kalodimos identified the mechanism of function of motor protein SecA, which uses chemical energy and converts it into mechanical energy. SecA is present only in bacteria and is not found in humans. SecA uses mechanical energy to secrete toxins and other harmful proteins to the exterior of the bacterium cell.

Once a bacterium infects a human or a host, some bacteria will use the SecA system to secrete specific bacteria proteins into the human body causing infections or diseases. Recent advances in NMR Spectroscopy a
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Contact: Peter Haigney
phaigney@andromeda.rutgers.edu
973-353-1663
Rutgers, the State University of New Jersey
20-Jul-2006


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