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Multiple quantum so...
Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
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- Antzutkin, Oleg (författare)
- Luleå tekniska universitet,Industriell miljö- och processteknik
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- Balbach, John J. (författare)
- Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda
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- Leapman, Richard D. (författare)
- Division of Bioengineering and Physical Science, Office of Research Services, National Institutes of Health, Bethesda
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- Rizzo, Nancy W. (författare)
- Division of Bioengineering and Physical Science, Office of Research Services, National Institutes of Health, Bethesda
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- Reed, Jennifer (författare)
- Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda
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- Tycko, Robert (författare)
- National Institutes of Health, Bethesda
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(creator_code:org_t)
- 2000-11-07
- 2000
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 97:24, s. 13045-13050
- Relaterad länk:
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http://www.pnas.org/...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Senile plaques associated with Alzheimer's disease contain deposits of fibrils formed by 39- to 43-residue β-amyloid peptides with possible neurotoxic effects. X-ray diffraction measurements on oriented fibril bundles have indicated an extended β-sheet structure for Alzheimer's β-amyloid fibrils and other amyloid fibrils, but the supramolecular organization of the β-sheets and other structural details are not well established because of the intrinsically noncrystalline, insoluble nature of amyloid fibrils. Here we report solid-state NMR measurements, using a multiple quantum (MQ) 13C NMR technique, that probe the β-sheet organization in fibrils formed by the full-length, 40-residue β-amyloid peptide (Aβ1-40). Although an antiparallel β-sheet organization often is assumed and is invoked in recent structural models for full-length β-amyloid fibrils, the MQNMR data indicate an in-register, parallel organization. This work provides site-specific, atomic-level structural constraints on full-length β-amyloid fibrils and applies MQNMR to a significant problem in structural biology.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Nyckelord
- Chemistry of Interfaces
- Gränsytors kemi
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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