Structural fingerprinting of protein aggregates by DNP-enhanced solid-state NMR at natural isotopic abundance

Adam N Smith, Katharina Märker, Talia Piretra, Jennifer C Boatz, Irina Matlahov, Ravindra B Kodali, Sabine Hediger, Patrick C A van der Wel, Gaël De Paëpe

OnderzoeksoutputAcademicpeer review

22 Citaten (Scopus)

Samenvatting

A pathological hallmark of Huntington's disease (HD) is the formation of neuronal protein deposits containing mutant huntingtin fragments with expanded polygluta-mine (polyQ) domains. 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 ap-proach for the structural fingerprinting of fibrils through ssNMR at natural isotopic abundance (NA). These methods will enable the spectroscopic fingerprint-ing of unlabeled (e.g. ex-vivo) protein aggregates and the extraction of valuable new long-range 13C - 13C distance constraints.

Originele taal-2English
Pagina's (van-tot)14576-14580
Aantal pagina's5
TijdschriftJournal of the American Chemical Society
Volume140
Nummer van het tijdschrift44
Vroegere onlinedatum2018
DOI's
StatusPublished - 7-nov.-2018
Extern gepubliceerdJa

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