High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin

Michael J. Tappin, Annalisa Pastore, Raymond S. Norton, John H. Freer, Iain D. Campbell

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55 Citations (Scopus)

Abstract

The 26-residue toxin from Staphylococcus aureus, δ-Hemolysin, is thought to act by traversing the plasma membrane. The structure of this peptide, in methanol solution, has been investigated by using high-resolution NMR in combination with molecular dynamics calculations. The1H NMR spectrum has been completely assigned, and it is shown that residues 2–20 form a relatively stable helix while the residues at the C-terminal end appear to be more flexible. The structures were calculated only from nuclear Overhauser effect data and standard bond lengths. It is shown that the results are consistent with3JNH-α CHcoupling constants and amide hydrogen exchange rates.

Original languageEnglish
Pages (from-to)1643-1647
Number of pages5
JournalBiochemistry
Volume27
Issue number5
DOIs
Publication statusPublished - 1 Mar 1988
Externally publishedYes

Cite this

Tappin, M. J., Pastore, A., Norton, R. S., Freer, J. H., & Campbell, I. D. (1988). High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin. Biochemistry, 27(5), 1643-1647. https://doi.org/10.1021/bi00405a038
Tappin, Michael J. ; Pastore, Annalisa ; Norton, Raymond S. ; Freer, John H. ; Campbell, Iain D. / High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin. In: Biochemistry. 1988 ; Vol. 27, No. 5. pp. 1643-1647.
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Tappin, MJ, Pastore, A, Norton, RS, Freer, JH & Campbell, ID 1988, 'High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin', Biochemistry, vol. 27, no. 5, pp. 1643-1647. https://doi.org/10.1021/bi00405a038

High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin. / Tappin, Michael J.; Pastore, Annalisa; Norton, Raymond S.; Freer, John H.; Campbell, Iain D.

In: Biochemistry, Vol. 27, No. 5, 01.03.1988, p. 1643-1647.

Research output: Contribution to journalArticleResearchpeer-review

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