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Protein 'filmed' while unfolding at atomic resolution
Date:2/11/2013

By combining low temperatures and NMR spectroscopy, the scientists visualized seven intermediate forms of the CylR2 protein while cooling it down from 25C to -16C. Their results show that the most instable intermediate form plays a key role in protein folding. The scientists' findings may contribute to a better understanding of how proteins adopt their structure and misfold during illness.

Whether Alzheimer's, Parkinson's or Huntington's Chorea all three diseases have one thing in common. They are caused by misfolded proteins that form insoluble clumps in the brains of affected patients and, finally, destroy their nerve cells. One of the most important questions in the biological sciences and medicine is thus: How do proteins the tools of living cells achieve or lose their three-dimensional structure. Because only if their amino acid chains are correctly folded, can proteins perform their tasks properly.

But what exactly happens when proteins fold or unfold was previously nearly impossible to investigate. With heat and pressure, proteins easily lose their shape and thus their function. However, such methods are not suitable for directly observing their unfolding process. The intermediate forms that occur in the course of protein folding are much too transient.

With a novel approach, researchers have now succeeded in "filming" the complex process of protein folding for the first time. Scientists at the Max Planck Institute for Biophysical Chemistry (MPIbpc) and the German Center for Neurodegenerative Diseases (DZNE) in Gttingen, together with their colleagues at the Polish Academy of Sciences in Warsaw and at the University of Warsaw, have rendered visible at atomic resolution how a protein progressively "loses its shape". In doing so, the researchers had pinned their hopes on low temperatures. "If a protein is slowly cooled down, its intermediate forms accumulate in larger quantities than in commonly used denaturation methods,
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Contact: Dr. Dirk Frger
presse@dzne.de
0049-228-433-02260
Helmholtz Association of German Research Centres
Source:Eurekalert

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