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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 Folding01:22

Protein Folding

Overview
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 Organization01:13

Protein Organization

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Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: Jun 6, 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

Intermolecular alignment in β2-microglobulin amyloid fibrils.

Galia T Debelouchina1, Geoffrey W Platt, Marvin J Bayro

  • 1Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

Journal of the American Chemical Society
|November 17, 2010
PubMed
Summary

Dialysis-related amyloidosis involves beta2-microglobulin (β2m) fibril deposition. Solid-state NMR reveals these β2m fibrils adopt a parallel, in-register structure, indicating significant protein reorganization from its native state.

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &beta;2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Last Updated: Jun 6, 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

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &beta;2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Dialysis-related amyloidosis is characterized by amyloid-like fibril deposition.
  • These fibrils are primarily composed of beta2-microglobulin (β2m).
  • In vitro formed β2m fibrils mimic disease-related fibrils and possess a significant β-sheet core.

Purpose of the Study:

  • To investigate the intrasheet arrangement of β2m fibrils.
  • To elucidate the structural organization of protein subunits within the fibrils.

Main Methods:

  • Utilized (15)N-(13)C MAS NMR correlation spectroscopy.
  • Employed a fibril sample from a mixture of isotopically labeled β2m monomers.
  • Incorporated Zero-Field Transverse Experimental Decay Optical Rotations (ZF-TEDOR) mixing for enhanced signal detection.

Main Results:

  • Observed intermolecular (15)N-(13)C backbone-to-backbone contacts with high resolution and sensitivity.
  • Results are consistent with a parallel, in-register arrangement of β2m subunits within the fibrils.
  • Demonstrated significant structural reorganization from the native β2m state to the fibril state.

Conclusions:

  • The study clarifies the fibril architecture of β2m.
  • Provides insights into the molecular mechanisms of dialysis-related amyloidosis.
  • Highlights the substantial conformational changes during protein misfolding and fibril formation.