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Solid-State NMR as a Probe of Amyloid Structure

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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 Alzheimer's 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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Keywords: Alzheimer's disease; Amyloid structure; magnetic resonance; prions; protein aggregation

Document Type: Research Article

Affiliations: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, (NIDDK) National Institutes of Health, Bldg. 5, Rm 112, Bethesda, Maryland 20892-0520, USA.

Publication date: 2006-03-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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