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Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
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Prion protein β2-α2 loop conformational landscape.

Enrico Caldarulo1,2, Alessandro Barducci3, Kurt Wüthrich4,5

  • 1Department of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zurich, CH-8093 Zurich, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|August 23, 2017
PubMed
Summary
This summary is machine-generated.

Researchers investigated the structural changes in the prion protein (PrP) linked to transmissible spongiform encephalopathies (TSEs). Using advanced computational methods, they mapped the free-energy landscape of a key PrP segment, revealing insights into disease mechanisms.

Keywords:
metadynamicsprionβ2–α2 loop

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Computational Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
  • The prion protein (PrP) undergoes a conformational change from its cellular form (PrPC) to an aggregated scrapie form (PrPSc).
  • Understanding PrPC's physiological function and the PrPC-to-PrPSc conversion mechanism is crucial.

Purpose of the Study:

  • To characterize the conformational free-energy surface of a specific mouse PrP segment (residues 121-231).
  • To investigate the role of the 167-170 loop, including the Y169A variant, in PrP structure and disease susceptibility.
  • To provide quantitative insights into the structural transition-related function of the PrP loop.

Main Methods:

  • Utilized a combination of Well-Tempered Ensemble (WTE) and Parallel Tempering (PT) schemes.
  • Employed Metadynamics (MetaD) simulations to explore the conformational landscape.
  • Analyzed an 11-residue polypeptide segment of mouse PrP(121-231), comparing wild-type with the Y169A variant.

Main Results:

  • Detailed conformational landscapes of the wild-type and Y169A mouse PrP(121-231) segment were generated.
  • The study identified key conformational states and transitions within the analyzed PrP region.
  • Quantitative insights into the structural dynamics of the [Formula: see text]2-[Formula: see text]2 loop were obtained.

Conclusions:

  • The generated conformational landscapes integrate with existing experimental data on PrP.
  • The findings offer a deeper understanding of the structural basis for PrP's role in TSEs.
  • This research elucidates the functional significance of the [Formula: see text]2-[Formula: see text]2 loop in prion protein structure and conversion.