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        <identifier>oai:figshare.com:article/33713959</identifier>
        <datestamp>2026-09-13T17:07:43Z</datestamp>
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          <dc:title>Data for Hydrogen Bonding in Alzheimer’s Amyloid-β Fibrils Probed by15N{17O} REAPDOR Solid-State NMR Spectroscopy</dc:title>
          <dc:creator>Juan Wei (498096)</dc:creator>
          <dc:creator>Oleg N. Antzutkin (1296813)</dc:creator>
          <dc:creator>Andrei V. Filippov (1753414)</dc:creator>
          <dc:creator>Dinu Iuga (1345257)</dc:creator>
          <dc:creator>Pui Yiu Lam (2033866)</dc:creator>
          <dc:creator>Mark P. Barrow (1756480)</dc:creator>
          <dc:creator>Ray Dupree (1356219)</dc:creator>
          <dc:creator>Steven P. Brown (1296819)</dc:creator>
          <dc:creator>Peter B. O'Connor (2535301)</dc:creator>
          <dc:subject>Hydrogen bonding</dc:subject>
          <dc:subject>Amyloid</dc:subject>
          <dc:subject>Alzheimer's disease -- Physiological aspects</dc:subject>
          <dc:subject>Migrated from ePrints</dc:subject>
          <dc:description>An exclusive label: 15N{17O} REAPDOR NMR was used to validate intermolecular C17O⋅⋅⋅H15N hydrogen bonding in Ac-Aβ(16–22)-NH2 (see scheme) and Aβ(11–25) amyloid fibrils, which are associated with Alzheimer's disease, by selectively labeling them with 17O and 15N. This method was effective for confirming the structure of these fibrils, and could be useful for a number of other biological samples.&lt;br&gt;&lt;br&gt;Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution FTICR-MS  All data are Bruker NMR data sets recorded by Oleg Antzutkin and Dinu Iuga</dc:description>
          <dc:date>2016-03-21T00:00:00Z</dc:date>
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          <dc:type>Dataset</dc:type>
          <dc:identifier>10.82444/warw.33713959.v1</dc:identifier>
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          <dc:rights>CC BY 4.0</dc:rights>
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