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Imaging Parkinson’s protein: NMR and EPR

A combined approach using nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy reveals details of the changes that occur in the protein α-synuclein in Parkinson’s disease.
The protein α-synuclein is found mainly in the brain, although it also occurs in heart tissue, muscles and elsewhere. It is present mainly at the tips of neurons in the presynaptic terminals. The protein is thought to play a critical role in Parkinson’s disease and other neurodegenerative disorders. Science already knows quite a lot about the structure of the protein within the Parkinson’s-typical amyloid deposits that apparently give rise to the symptoms of the disease. However, until now nothing was known about the original state of the protein in the healthy cell.
Now, researchers at the Leibniz-Institut für Molekulare Pharmakologie (FMP) in Berlin, Germany, have used NMR and EPR together to visualize for the first time the healthy form of this protein in healthy cells. Paradoxically, it seems to exist in an unstructured state one that might in a different protein under different circumstances be described as misfolded and perhaps itself a cause of disease. The team describes their findings in two papers published in the journal Nature and its sibling publication Nature Communications. It is also now obvious that the structure of this protein changes dramatically through the course of the disease.

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