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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Related Experiment Video

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Cellular prion protein conformation and function.

Fred F Damberger1, Barbara Christen, Daniel R Pérez

  • 1Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Schafmattstrasse 20, CH-8093 Zurich, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|October 12, 2011
PubMed
Summary

Cellular prion protein (PrP(C)) exhibits conformational flexibility. Specific mutations in mouse PrP(C) reveal distinct structural states, aiding research into prion protein function.

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Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Area of Science:

  • Structural Biology
  • Biochemistry
  • Neuroscience

Background:

  • Cellular prion protein (PrP(C)) structure is highly conserved across mammals.
  • Species variations exist in a surface epitope involving the β2-α2 loop.
  • These variations are linked to dynamic conformational equilibria.

Purpose of the Study:

  • To investigate the role of Tyr169 in mouse PrP(C) conformational dynamics.
  • To identify the specific conformations involved in the local exchange.
  • To provide structural insights for future studies on PrP(C) function.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) structure determination of designed mouse PrP(121-231) variants.
  • NMR structure determination of wild-type mouse PrP(121-231) at different temperatures.
  • Analysis of NMR signal exchange effects.

Main Results:

  • Exchange of Tyr169 with Ala or Gly eliminated conformational polymorphism in mouse PrP(C).
  • Exchange with Phe preserved the polymorphism.
  • Two distinct, exchanging structures of wild-type mouse PrP(C) were identified, differing in solvent-exposed epitopes near the β2-α2 loop.

Conclusions:

  • The study elucidates the structural basis of conformational dynamics in mouse PrP(C).
  • Specific residues, like Tyr169, significantly influence PrP(C) conformational flexibility.
  • These findings offer a structural foundation for investigating the physiological role of PrP(C).