A glimpse of a possible amyloidogenic intermediate of transthyretin

Kai Liu, Ho S. Cho, Hilal A. Lashuel, Jeffery W. Kelly, David E. Wemmer

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132 Citations (Scopus)


Studies have indicated that partially unfolded states occur under conditions that favor amyloid formation by transthyretin (TTR), as well as other amyloidogenic proteins. In this study, we used hydrogen exchange measurements to show that there is selective destabilization of one half of the β-sandwich structure of TTR under such conditions. This provides more direct information about conformational fluctuations than previously available, and will facilitate design of future experiments to probe the intermediates critical to amyloid formation.

Original languageEnglish
Pages (from-to)754-757
Number of pages4
JournalNature Structural Biology
Issue number9
Publication statusPublished - 1 Sep 2000
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Liu, K., Cho, H. S., Lashuel, H. A., Kelly, J. W., & Wemmer, D. E. (2000). A glimpse of a possible amyloidogenic intermediate of transthyretin. Nature Structural Biology, 7(9), 754-757. https://doi.org/10.1038/78980