Researchers at the Max Planck Institute for Biophysical Chemistry and the German Center for Neurodegenerative Diseases in Göttingen – in collaboration with Polish colleagues – have now “filmed” how a protein gradually unfolds for the first time.
“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.
© Zweckstetter, Max Planck Institute for Biophysical Chemistry & German Center for Neurodegenerative Diseases
By combining low temperatures and NMR spectroscopy, the scientists visualized seven intermediate forms of the CylR2 protein while cooling it down from 25°C to - 16°C. 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. (Nature Chemical Biology, 10. February 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.
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 25°C to -16°C 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’s findings may help to gain deeper insights into how proteins assume their spatial structure and why intermediate forms of certain proteins misfold in the event of illness. (cr)Original Publication
Dr. Dirk Förger | Max-Planck-Institute
Further reports about: > Alzheimer > Chemical Biology > CylR2 > DZNE > German language > MPIbpc > MR spectroscopy > Max Planck Institute > NMR spectroscopy > Nature Chemical Biology > Protein > atomic resolution > chemical engineering > nerve cell > neurodegenerative diseases > protein folding > protein structures > synthetic biology
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