Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR

Nicolas L. Fawzi, Jinfa Ying, Rodolfo Ghirlando, Dennis A. Torchia and G. Marius Clore ()
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Nicolas L. Fawzi: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Jinfa Ying: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Rodolfo Ghirlando: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Dennis A. Torchia: National Institute of Dental and Craniofacial Research, National Institutes of Health
G. Marius Clore: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health

Nature, 2011, vol. 480, issue 7376, 268-272

Abstract: Visibility cloak for hidden proteins When proteins associate with larger structures such as polymers, membranes or solid supports, they usually become 'invisible' to the techniques used to visualize them as free molecules in solution. Marius Clore and colleagues have now developed a new technique of solution nuclear magnetic resonance that can probe such exchange phenomena at atomic resolution. Termed dark-state exchange saturation transfer (DEST), the procedure is demonstrated here by following the aggregation of the amyloid-β monomers implicated in Alzheimer's disease. It should also be adaptable to many of the supramolecular systems encountered in biological systems and materials science.

Date: 2011
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DOI: 10.1038/nature10577

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