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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 studies of amyloid fibril structure
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. robertty@mail.nih.gov
Annual Review of Physical Chemistry
|January 12, 2011
Summary
Solid-state nuclear magnetic resonance (NMR) reveals detailed structures of amyloid fibrils, crucial for understanding neurodegenerative diseases like Alzheimer's. This review covers recent NMR advancements and their application to disease-related protein aggregates.
Area of Science:
- Biophysics
- Structural Biology
- Neuroscience
Background:
- Amyloid fibrils are implicated in neurodegenerative diseases and represent alternative protein structures.
- Understanding the molecular structure of amyloid fibrils is key to disease research.
- Solid-state nuclear magnetic resonance (NMR) offers unique capabilities for studying these structures.
Purpose of the Study:
- To review recent advancements in solid-state NMR techniques for amyloid fibril research.
- To highlight the application of solid-state NMR to Alzheimer's disease fibrils and prion fibrils.
- To discuss the development of molecular models based on NMR-derived structural constraints.
Main Methods:
- Solid-state nuclear magnetic resonance (NMR) spectroscopy.
- Analysis of structural constraints from NMR data.
- Development of molecular models for amyloid fibrils.
Main Results:
- Solid-state NMR provides high-resolution structural information on amyloid fibrils.
- Detailed molecular models can be constructed using NMR constraints.
- Recent technological advancements enhance NMR's utility in this field.
Conclusions:
- Solid-state NMR is a powerful tool for elucidating amyloid fibril structures.
- This technique is vital for advancing our understanding of amyloid-related diseases.
- Continued development in NMR methods will further benefit structural biology and disease research.
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...