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Prior studies have shown the strengths of solid-state NMR (ssNMR) to probe the atomic structure of such aggregates, but have required in vitro isotopic labeling. Herein, we present an approach for the structural fingerprinting of fibrils through ssNMR at natural isotopic abundance (NA). These methods will enable the spectroscopic fingerprinting of unlabeled (e.g., ex vivo) protein aggregates and the extraction of valuable new long-range 13C\u201313C distance constraints.<\/jats:p>","DOI":"10.1021\/jacs.8b09002","type":"journal-article","created":{"date-parts":[[2018,10,19]],"date-time":"2018-10-19T14:38:40Z","timestamp":1539959920000},"page":"14576-14580","source":"Crossref","is-referenced-by-count":30,"title":["Structural\nFingerprinting of Protein Aggregates by\nDynamic Nuclear Polarization-Enhanced Solid-State NMR at Natural Isotopic\nAbundance"],"prefix":"10.1021","volume":"140","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1373-1115","authenticated-orcid":true,"given":"Adam N.","family":"Smith","sequence":"first","affiliation":[{"name":"Univ. 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