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

doi:10.1021/bi00405a038

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

Research output: Contribution to journal › Article › Research › peer-review

60 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 with³J_NH-_α _CHcoupling constants and amide hydrogen exchange rates.

Original language	English
Pages (from-to)	1643-1647
Number of pages	5
Journal	Biochemistry
Volume	27
Issue number	5
DOIs	https://doi.org/10.1021/bi00405a038
Publication status	Published - 1 Mar 1988
Externally published	Yes

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10.1021/bi00405a038

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title = "High-resolution1H NMR Study of the Solution Structure of δ-Hemolysin",

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.",

author = "Tappin, {Michael J.} and Annalisa Pastore and Norton, {Raymond S.} and Freer, {John H.} and Campbell, {Iain D.}",

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AU - Campbell, Iain D.

PY - 1988/3/1

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N2 - 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.

AB - 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.

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JO - Biochemistry

JF - Biochemistry

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

Abstract

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