Ontology highlight
ABSTRACT:
SUBMITTER: Smith AN
PROVIDER: S-EPMC6287890 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Smith Adam N AN Märker Katharina K Piretra Talia T Boatz Jennifer C JC Matlahov Irina I Kodali Ravindra R Hediger Sabine S van der Wel Patrick C A PCA De Paëpe Gaël G
Journal of the American Chemical Society 20181026 44
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 ...[more]