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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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Amyloid Fibrils03:03

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Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Protein Folding01:25

Protein Folding

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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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Related Experiment Video

Updated: Apr 22, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Kinetic intermediates in amyloid assembly.

Chen Liang1, Rong Ni, Jillian E Smith

  • 1Departments of Chemistry and Biology, Emory University , Atlanta, Georgia 30322, United States.

Journal of the American Chemical Society
|October 15, 2014
PubMed
Summary

Alzheimer's disease amyloid peptide assemblies form via conformational transitions, not Ostwald ripening. New mechanisms for Alzheimer's nucleation pathways were uncovered using advanced structural methods.

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Amyloid assemblies are implicated in Alzheimer's disease pathogenesis.
  • The typical model for amyloid growth is Ostwald-like ripening.

Purpose of the Study:

  • To investigate the nucleation mechanism of the Dutch mutant Aβ peptide in Alzheimer's disease.
  • To elucidate the structural intermediates during amyloid assembly.

Main Methods:

  • Isotope-edited Infrared (IR) spectroscopy
  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy

Main Results:

  • Observed a series of conformational transitions during nucleation, contrasting with Ostwald-like ripening.
  • Identified unexpected strand orientation in intermediate assemblies.
  • Characterized the progressive assembly pathway of the amyloid core.

Conclusions:

  • The nucleation of the Dutch mutant Aβ peptide involves distinct conformational transitions.
  • These findings suggest novel nucleation mechanisms for amyloid formation in Alzheimer's disease.
  • The progressive assembly pathway provides new insights into amyloid structure.