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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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...
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

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Related Experiment Video

Updated: Jun 5, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Conformational conversion during amyloid formation at atomic resolution.

Timo Eichner1, Arnout P Kalverda, Gary S Thompson

  • 1Astbury Centre for Structural Molecular Biology and Institute of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK.

Molecular Cell
|January 25, 2011
PubMed
Summary
This summary is machine-generated.

Partially folded amyloidogenic intermediates initiate protein aggregation. Researchers determined the high-resolution structure of a β(2)-microglobulin intermediate (ΔN6), revealing structural changes that enhance its amyloidogenic potential and ability to convert wild-type proteins.

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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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Last Updated: Jun 5, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

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

Published on: March 21, 2025

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Misfolding Diseases

Background:

  • Amyloid assembly is initiated by partially folded protein species.
  • Structural and dynamic features of these intermediates are not well understood.
  • Understanding these intermediates is crucial for elucidating aggregation mechanisms.

Purpose of the Study:

  • Determine the high-resolution solution structure of a nonnative amyloidogenic intermediate.
  • Investigate the structural and dynamic basis of its increased amyloidogenic potential.
  • Elucidate the mechanism by which this intermediate converts wild-type proteins into an amyloidogenic conformation.

Main Methods:

  • Utilized a truncation variant, ΔN6, of β(2)-microglobulin (β(2)m).
  • Determined the solution structure of the ΔN6 intermediate using high-resolution techniques.
  • Analyzed pH-dependent backbone dynamics on a microsecond-millisecond timescale.

Main Results:

  • Revealed a major repacking of the hydrophobic core in ΔN6 to accommodate a nonnative peptidyl-prolyl trans-isomer.
  • Observed enhanced backbone dynamics in ΔN6, correlating with increased amyloidogenic potential.
  • Demonstrated that catalytic amounts of ΔN6 can convert nonamyloidogenic human wild-type β(2)m (Hβ(2)m) into an amyloidogenic conformation.

Conclusions:

  • The structure of the ΔN6 intermediate provides insights into the molecular basis of amyloid formation.
  • Specific structural rearrangements and dynamics contribute to the high amyloidogenic potential of this intermediate.
  • Catalytic conversion of wild-type β(2)m by the intermediate offers a mechanism for seeding amyloid aggregation.