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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...

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Updated: May 31, 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

Solid-state NMR of amyloid membrane interactions.

John D Gehman1, Frances Separovic

  • 1School of Chemistry, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia. jgehman@unimelb.edu.au

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2011
PubMed
Summary
This summary is machine-generated.

This study details solid-state Nuclear Magnetic Resonance (NMR) methods for analyzing amyloid-beta (Aβ) peptides in phospholipid vesicles. It provides protocols for sample preparation and parameter optimization for improved solid-state NMR studies of misfolding diseases.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Published on: September 17, 2017

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Neuroscience

Background:

  • Solid-state NMR (ssNMR) offers unique insights into biomolecular structures but requires meticulous parameter optimization.
  • Semi-solid samples, like phospholipid vesicles, present challenges in ssNMR due to their complex nature.
  • Amyloid-beta (Aβ) peptides in vesicles are crucial for understanding misfolding diseases.

Purpose of the Study:

  • To describe protocols for preparing multilamellar vesicles for ssNMR studies of Aβ peptides.
  • To outline procedures for optimizing critical experimental parameters in ssNMR of these systems.
  • To enhance the application of ssNMR in studying membrane-associated peptides and proteins involved in misfolding diseases.

Main Methods:

  • Development of protocols for multilamellar vesicle preparation.
  • Optimization of spectral widths, delay times, and field strengths for (31)P, (2)H, and (13)C NMR spectroscopy.
  • Application of solid-state NMR techniques to Aβ peptide-lipid systems.

Main Results:

  • Established robust protocols for preparing semi-solid vesicle samples suitable for ssNMR.
  • Identified optimal experimental parameters for enhanced spectral resolution and sensitivity.
  • Demonstrated the feasibility of detailed structural analysis of Aβ peptides within a membrane-mimetic environment.

Conclusions:

  • The described protocols and optimization strategies facilitate advanced solid-state NMR investigations of Aβ peptides in phospholipid vesicles.
  • This work provides a foundation for further studies into the structural basis of Aβ-related misfolding diseases using ssNMR.
  • Optimized ssNMR methods are essential for overcoming the challenges associated with studying complex semi-solid biological systems.