Abstract
Solid state nuclear magnetic resonance (NMR) has developed into one of the most informative and direct experimental approaches to the characterization of the molecular structures of amyloid fibrils, including those associated with Alzheimers disease. In this article, essential aspects of solid state NMR methods are described briefly and results obtained to date regarding the supramolecular organization of amyloid fibrils and the conformations of peptides within amyloid fibrils are reviewed.
Keywords: Amyloid structure, Alzheimer's disease, prions, protein aggregation, magnetic resonance
Protein & Peptide Letters
Title: Solid-State NMR as a Probe of Amyloid Structure
Volume: 13 Issue: 3
Author(s): Robert Tycko
Affiliation:
Keywords: Amyloid structure, Alzheimer's disease, prions, protein aggregation, magnetic resonance
Abstract: Solid state nuclear magnetic resonance (NMR) has developed into one of the most informative and direct experimental approaches to the characterization of the molecular structures of amyloid fibrils, including those associated with Alzheimers disease. In this article, essential aspects of solid state NMR methods are described briefly and results obtained to date regarding the supramolecular organization of amyloid fibrils and the conformations of peptides within amyloid fibrils are reviewed.
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Cite this article as:
Tycko Robert, Solid-State NMR as a Probe of Amyloid Structure, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338470
DOI https://dx.doi.org/10.2174/092986606775338470 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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