Understanding the Structure of Tau Protein in Alzheimer's Disease
Author Information
Author(s): Mukrasch Marco D, Bibow Stefan, Korukottu Jegannath, Jeganathan Sadasivam, Biernat Jacek, Griesinger Christian, Mandelkow Eckhard, Zweckstetter Markus
Primary Institution: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany
Hypothesis
Can nuclear magnetic resonance (NMR) spectroscopy provide detailed insights into the structural polymorphism of the tau protein?
Conclusion
NMR spectroscopy reveals that the tau protein is highly dynamic in solution and has an intricate network of transient long-range contacts important for its aggregation.
Supporting Evidence
- NMR spectroscopy can provide detailed insight into the structural polymorphism of very large nonglobular proteins.
- The study reveals that 441-residue tau is highly dynamic in solution.
- Unique insights into the interaction of tau with microtubules were obtained through single-residue NMR analysis.
- The findings suggest that tau's structural properties are crucial for its function and aggregation in Alzheimer's disease.
Takeaway
The tau protein, which is important in Alzheimer's disease, can change shape a lot, and scientists used a special technique to see how it moves and interacts with other parts of the cell.
Methodology
The study used nuclear magnetic resonance (NMR) spectroscopy to analyze the structure and dynamics of the tau protein at single residue resolution.
Limitations
The study's findings may be limited by the inherent challenges of studying large, natively unfolded proteins using NMR.
Digital Object Identifier (DOI)
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