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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Solid-state NMR techniques for the structural determination of amyloid fibrils
1Department of Chemistry, National Taiwan University, Taipei, Taiwan. chanjcc@ntu.edu.tw
Topics in Current Chemistry
|June 2, 2011
Summary
Solid-state Nuclear Magnetic Resonance (NMR) techniques are powerful tools for studying amyloid fibrils. This review highlights key NMR methods and their practical applications for analyzing biological solids.
Area of Science:
- Biophysics
- Biochemistry
- Materials Science
Background:
- Amyloid fibrils are protein aggregates implicated in various diseases.
- Understanding their structure is crucial for developing therapeutic strategies.
- Solid-state Nuclear Magnetic Resonance (NMR) offers unique insights into these challenging systems.
Purpose of the Study:
- To review and categorize solid-state NMR techniques applicable to amyloid fibril research.
- To emphasize the practical aspects and power of NMR for studying biological unoriented solids.
- To provide a comprehensive overview of methods developed up to the end of 2010.
Main Methods:
- Homonuclear dipolar recoupling and polarization transfer via J-coupling.
- Heteronuclear dipolar recoupling.
- Correlation spectroscopy, recoupling of chemical shift anisotropy, and tensor correlation.
Main Results:
- Detailed discussion of five major categories of solid-state NMR techniques.
- Emphasis on the practical implementation and advantages of each technique.
- Demonstration of NMR's capability in characterizing the structure of amyloid fibrils.
Conclusions:
- Solid-state NMR is a versatile and powerful technique for investigating amyloid fibril structure.
- The reviewed techniques provide essential tools for advancing research in neurodegenerative diseases.
- Further development of NMR methods will continue to enhance our understanding of biological solids.
Related Concept Videos
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...
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...