1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin

J. A. Wilce, D. J. Craik, N. Ede, D. C. Jackson, G. Schreiber

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Two synthetic peptides corresponding to N-terminal fragments of human and chicken transthyretin have been synthesized and their structures examined in solution using 1H NMR spectroscopy. Complete sequence-specific assignments obtained for the two peptides are reported together with coupling constant and nuclear Overhauser data. The peptides were found to adopt random-coil conformations in aqueous solution. This is consistent with findings from X-ray structures of the native human transthyretin where the N-terminal region could not be defined, presumably because of conformational disorder.

Original languageEnglish
Pages (from-to)1153-1159
Number of pages7
JournalBiochemistry and Molecular Biology International
Issue number6
Publication statusPublished - 1 Dec 1995
Externally publishedYes

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