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

such as heat, pressure, or urea. We hoped that these quantities would be sufficient to examine the intermediate forms with nuclear magnetic resonance (NMR) spectroscopy," said Markus Zweckstetter, head of the research groups "Protein Structure Determination using MNR" at the MPIbpc and "Structural Biology in Dementia" at the DZNE in Gttingen.

How a protein loses its shape

As research object, Zweckstetter's team chose a key protein for toxin production in Enterococcus faecalis, a pathogen frequently encountered in hospitals where it particularly infects patients with a weak immune system. But that is not the only reason why the so-called CylR2 protein is interesting. Some time ago, researchers working with Stefan Becker at the MPIbpc succeeded in elucidating its structure, which shows: Its three-dimensional shape makes CylR2 a particular promising candidate for the scientists' approach. "ClyR2 is a relatively small protein composed of two identical subunits. This gave us a great chance to be able to visualize the individual stages of its unfolding process in the test tube," explained the chemists Mariusz and Lukasz Jaremko.

Stefan Becker's group undertook the first step: to prepare a sufficient quantity of the protein in the laboratory. Subsequently, the two chemists cooled the protein successively from 25C to -16C and examined its intermediate forms with NMR spectroscopy. They achieved what they had hoped for: Their "film clip" shows at atomic resolution how the protein gradually unfolds. The structural biologist Markus Zweckstetter describes exactly what happens in this process: "We clearly see how the CylR2 protein ultimately splits into its two subunits. The individual subunit is initially relatively stable. With further cooling, the protein continues to unfold and at -16 C it is extremely instable and dynamic. This instable protein form provides the seed for folding and can also be the "trigger" for misfolding." The scientist
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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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