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  Structural characterization of polyglutamine fibrils by solid-state NMR spectroscopy

Schneider, R., Schumacher, M. C., Müeller, H., Nand, D., Klaukien, V., Heise, H., et al. (2011). Structural characterization of polyglutamine fibrils by solid-state NMR spectroscopy. Journal of molecular biology, 412(1), 121-136. doi:10.1016/j.jmb.2011.06.045.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-63DE-6 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-63DF-4
Genre: Journal Article

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Schneider, R., Author
Schumacher, M. C., Author
Müeller, H., Author
Nand, D., Author
Klaukien, V., Author
Heise, H., Author
Riedel, D., Author
Wolf, G., Author
Behrmann, E.1, Author
Raunser, S., Author
Seidel, R., Author
Engelhard, M., Author
Baldus, M., Author
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1External Organizations, ou_persistent22              

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Free keywords: Magnetic Resonance Spectroscopy/*methods Microscopy, Electron Peptides/chemical synthesis/*chemistry
 Abstract: Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides below, at, and above the toxicity limit of around 37 glutamine residues using solid-state NMR and electron microscopy. Experimental data are consistent with a dry fibril core of at least 70-80 A in width for all constructs. Solid-state NMR dipolar correlation experiments reveal a largely beta-strand character of all samples and point to tight interdigitation of hydrogen-bonded glutamine side chains from different sheets. Two approximately equally frequent populations of glutamine residues with distinct sets of chemical shifts are found, consistent with local backbone dihedral angles compensating for beta-strand twist or with two distinct sets of side-chain conformations. Peptides comprising 15 glutamine residues are present as single extended beta-strands. Data obtained for longer constructs are most compatible with a superpleated arrangement with individual molecules contributing beta-strands to more than one sheet and an antiparallel assembly of strands within beta-sheets.

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 Dates: 2011
 Publication Status: Issued
 Pages: -
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 Rev. Type: -
 Identifiers: Other: 21763317
DOI: 10.1016/j.jmb.2011.06.045
ISSN: 1089-8638 (Electronic)
ISSN: 0022-2836 (Linking)
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Title: Journal of molecular biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 412 (1) Sequence Number: - Start / End Page: 121 - 136 Identifier: -