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

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

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
Volume36
Issue number6
Publication statusPublished - 1 Dec 1995
Externally publishedYes

Cite this

Wilce, J. A. ; Craik, D. J. ; Ede, N. ; Jackson, D. C. ; Schreiber, G. / 1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin. In: Biochemistry and Molecular Biology International. 1995 ; Vol. 36, No. 6. pp. 1153-1159.
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1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin. / Wilce, J. A.; Craik, D. J.; Ede, N.; Jackson, D. C.; Schreiber, G.

In: Biochemistry and Molecular Biology International, Vol. 36, No. 6, 01.12.1995, p. 1153-1159.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Wilce, J. A.

AU - Craik, D. J.

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AU - Jackson, D. C.

AU - Schreiber, G.

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