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000016612 0247_ $$2DOI$$a10.1016/j.jmb.2011.06.045
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000016612 084__ $$2WoS$$aBiochemistry & Molecular Biology
000016612 1001_ $$0P:(DE-HGF)0$$aSchneider, R.$$b0
000016612 245__ $$aStructural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy
000016612 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2011
000016612 300__ $$a121 - 136
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000016612 440_0 $$03552$$aJournal of Molecular Biology$$v412$$x0022-2836$$y1
000016612 500__ $$3POF3_Assignment on 2016-02-29
000016612 500__ $$aThis work was supported by the Deutsche Forschungsgemeinschaft (Grant RA 1781/1-1), the Max Planck Society, the Fonds der chemischen Industrie (Grant 684052), and Netherlands Organisation for Scientific Research (Grant 700.26.121). R.S. thanks the Deutsche Forschungsgemeinschaft graduate school 782 "Spectroscopy and Dynamics of Molecular Coils and Aggregates" for a PhD fellowship.
000016612 520__ $$aProtein 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 Å in width for all constructs. Solid-state NMR dipolar correlation experiments reveal a largely β-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 β-strand twist or with two distinct sets of side-chain conformations. Peptides comprising 15 glutamine residues are present as single extended β-strands. Data obtained for longer constructs are most compatible with a superpleated arrangement with individual molecules contributing β-strands to more than one sheet and an antiparallel assembly of strands within β-sheets.
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000016612 65320 $$2Author$$aamyloid fibrils
000016612 65320 $$2Author$$aHuntington's disease
000016612 65320 $$2Author$$aaggregation
000016612 65320 $$2Author$$apolyglutamine
000016612 65320 $$2Author$$asolid-state NMR
000016612 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy: methods
000016612 650_2 $$2MeSH$$aMicroscopy, Electron
000016612 650_2 $$2MeSH$$aPeptides: chemical synthesis
000016612 650_2 $$2MeSH$$aPeptides: chemistry
000016612 650_7 $$00$$2NLM Chemicals$$aPeptides
000016612 650_7 $$026700-71-0$$2NLM Chemicals$$apolyglutamine
000016612 650_7 $$2WoSType$$aJ
000016612 7001_ $$0P:(DE-HGF)0$$aSchumacher, M.C.$$b1
000016612 7001_ $$0P:(DE-Juel1)VDB24932$$aMueller, H.$$b2$$uFZJ
000016612 7001_ $$0P:(DE-HGF)0$$aNand, D.$$b3
000016612 7001_ $$0P:(DE-HGF)0$$aKlaukien, V.$$b4
000016612 7001_ $$0P:(DE-Juel1)VDB77857$$aHeise, H.$$b5$$uFZJ
000016612 7001_ $$0P:(DE-HGF)0$$aRiedel, D.$$b6
000016612 7001_ $$0P:(DE-HGF)0$$aWolf, G.$$b7
000016612 7001_ $$0P:(DE-HGF)0$$aBehrmann, E.$$b8
000016612 7001_ $$0P:(DE-HGF)0$$aRaunser, S.$$b9
000016612 7001_ $$0P:(DE-HGF)0$$aSeidel, R.$$b10
000016612 7001_ $$0P:(DE-HGF)0$$aEngelhard, M.$$b11
000016612 7001_ $$0P:(DE-HGF)0$$aBaldus, M.$$b12
000016612 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2011.06.045$$gVol. 412, p. 121 - 136$$p121 - 136$$q412<121 - 136$$tJournal of molecular biology$$v412$$x0022-2836$$y2011
000016612 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2011.06.045
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