A pathological hallmark
of Huntington’s disease (HD) is
the formation of neuronal protein deposits containing mutant huntingtin
fragments with expanded polyglutamine (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 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–13C distance constraints.
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