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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Protein Folding01:25

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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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Protein Folding01:22

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Protein Folding01:22

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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Rapid Generation of Amyloid from Native Proteins In vitro
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A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.

Theodoros K Karamanos1, Clare L Pashley1, Arnout P Kalverda1

  • 1Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, University of Leeds , Leeds LS2 9JT, U.K.

Journal of the American Chemical Society
|April 28, 2016
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Protein misfolding and amyloid assembly are linked to transient folding intermediates. Subtle changes in protein dynamics, not folding mechanisms, dictate amyloidogenicity, preventing harmful protein aggregation.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Protein folding and misfolding dynamics are critical for amyloid assembly.
  • Transient folding intermediates are implicated in amyloid aggregation but are difficult to study.
  • Amyloid diseases arise from protein misfolding and aggregation.

Purpose of the Study:

  • To investigate the folding pathway of amyloidogenic and nonamyloidogenic beta2-microglobulin (β2m) variants at atomic resolution.
  • To understand how subtle changes in protein dynamics influence amyloid formation.
  • To elucidate the role of transient intermediates in protein aggregation.

Main Methods:

  • Utilized nonuniformly sampled Nuclear Magnetic Resonance (NMR) methods for detailed structural characterization.
  • Analyzed the folding pathways of wild-type and variant β2m.
  • Quantified the population of key folding intermediates.

Main Results:

  • Both amyloidogenic and nonamyloidogenic β2m variants fold through common intermediate states.
  • Amyloid formation was inhibited by a decreased population of the aggregation-prone ITrans state.
  • A less stable, more dynamic intermediate species was populated in nonamyloidogenic variants, increasing the energy barrier for assembly.
  • Subtle alterations in conformational dynamics significantly impact protein amyloidogenicity.

Conclusions:

  • Protein amyloidogenicity is determined by conformational dynamics, not necessarily by a perturbed folding mechanism.
  • Targeting specific transient intermediates offers a potential strategy to inhibit amyloid assembly.
  • Understanding protein dynamics is key to deciphering the basis of amyloid diseases.