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Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Amyloid Fibrils03:03

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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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Amyloid Fibrils03:03

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Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
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Prion protein and its conformational conversion: a structural perspective.

Witold K Surewicz1, Marcin I Apostol

  • 1Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44120, USA. wks3@case.edu

Topics in Current Chemistry
|June 2, 2011
PubMed
Summary
This summary is machine-generated.

Prion diseases involve the misfolding of cellular prion protein (PrP(C)) into infectious PrP(Sc). This study explores the structural basis of this conversion and prion infectivity.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Prion diseases are linked to the misfolding of the cellular prion protein (PrP(C)) into an abnormal isoform (PrP(Sc)).
  • The "protein-only" model posits PrP(Sc) as the infectious agent, supported by increasing evidence.
  • Mechanistic and structural details of prion protein conversion remain incompletely understood.

Purpose of the Study:

  • To review recent advancements in understanding the biophysical and biochemical aspects of prion diseases.
  • To focus on the structural basis of prion protein conversion and the origins of prion strains.
  • To investigate the in vitro generation of prion infectivity from recombinant PrP.

Main Methods:

  • Review of recent literature on prion disease pathogenesis.
  • Analysis of structural data concerning PrP(C) and PrP(Sc) conformations.
  • Examination of studies on in vitro prion replication using recombinant PrP.

Main Results:

  • PrP(C) is monomeric and alpha-helical, while PrP(Sc) is oligomeric and beta-sheet rich.
  • Structural differences underpin the distinct properties of prion strains.
  • In vitro conversion of recombinant PrP into infectious prions has been achieved.

Conclusions:

  • Understanding the structural conversion of PrP is crucial for elucidating prion disease mechanisms.
  • The structural basis of prion strains is key to their distinct pathologies.
  • In vitro prion generation provides a powerful tool for studying prion infectivity.