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Updated: May 18, 2026
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization
Raimon Sabaté1, Salvador Ventura
1Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
Methods in Molecular Biology (Clifton, N.J.)
|September 19, 2012
Summary
Protein aggregate formation, common in dementia and diabetes, involves self-assembly into amyloid fibrils. This study details methods to detect the common cross-β-sheet structure found in these toxic protein assemblies.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Protein aggregate formation is implicated in prevalent human diseases like dementia and diabetes.
- The toxic mechanism often involves the self-assembly of soluble proteins into insoluble amyloid fibrils.
- These amyloid fibrils share a common cross-β-sheet supersecondary structure.
Purpose of the Study:
- To describe commonly used methods for analyzing the cross-β-sheet structure.
- To provide a detailed overview of techniques for detecting and characterizing amyloid fibrils.
Main Methods:
- Description of established analytical techniques for structural analysis.
- Focus on methods that identify cross-β-sheet conformational signatures.
- Discussion of techniques for screening protein samples for amyloid fibrils.
Main Results:
- Detailed explanation of multiple methods for analyzing protein supersecondary structure.
- Highlighting the utility of cross-β-sheet signatures for amyloid detection.
- Providing a comprehensive guide to current analytical approaches.
Conclusions:
- The cross-β-sheet conformation is a ubiquitous feature of toxic protein aggregates.
- Standardized methods are crucial for detecting, characterizing, and screening amyloid fibrils.
- Understanding these structures aids in the study of protein misfolding diseases.
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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, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid 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 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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01:25Protein Folding
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