Similar folds with different stabilization mechanisms: the cases of prion and doppel proteins
2006
Comparing Prion and Doppel Proteins
publication
Evidence: moderate
Author Information
Author(s): Colacino Stefano, Tiana Guido, Colombo Giorgio
Primary Institution: Istituto di Chimica del Riconoscimento Molecolare, CNR
Hypothesis
What are the molecular determinants that lead to different stabilization mechanisms in Prion and Doppel proteins?
Conclusion
The study found that Doppel has a more stable core than Prion, which affects their folding and misfolding behaviors.
Supporting Evidence
- Doppel has a higher stabilization energy concentration than Prion.
- The stabilization core of Doppel remains stable at higher temperatures, unlike Prion.
- Prion can misfold into various aggregation-prone conformations, while Doppel cannot.
Takeaway
Prion and Doppel proteins look similar but behave differently because their internal structures are stabilized in different ways.
Methodology
The study used long time scale explicit solvent, all-atom molecular dynamics simulations to analyze the proteins.
Digital Object Identifier (DOI)
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