“Snapshot” of the unfolding of the CylR2 protein from Enterococcus faecalis. If the protein is cooled from 25°C to -16°C, it successively breaks down into its two identical subunits. The latter are initially stable, but at -16°C they form an instable, dynamic protein form, which plays a key role in folding. (Credit: Image courtesy of Max Planck Institute for Biophysical Chemistry)

Protein ‘Filmed’ While Unfolding at Atomic Resolution

Feb. 11, 2013 — 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.

Read more: Protein 'filmed' while unfolding at atomic resolution — Science Daily.

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