Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

@article{Jaroniec2002MolecularCO,
  title={Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.},
  author={Christopher P Jaroniec and Cait E. MacPhee and Nathan S. Astrof and Christopher M. Dobson and Robert G Griffin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 26},
  pages={16748-53}
}
The molecular conformation of peptide fragment 105-115 of transthyretin, TTR(105-115), previously shown to form amyloid fibrils in vitro, has been determined by magic-angle spinning solid-state NMR spectroscopy. 13C and 15N linewidth measurements indicate that TTR(105-115) forms a highly ordered structure with each amino acid in a unique environment. 2D 13C-13C and 15N-13C-13C chemical shift correlation experiments, performed on three fibril samples uniformly 13C,15N-labeled in consecutive… CONTINUE READING
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