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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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

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