Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones

Paul R. Gooley; John W. Blunt; Raymond S. Norton

doi:10.1016/0014-5793(84)81068-6

Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones

Paul R. Gooley, John W. Blunt, Raymond S. Norton

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

26 Citations (Scopus)

Abstract

High-resolution ¹H NMR spectra at 300 MHz of the polypeptide cardiac stimulants anthopIeurin-A and Anemonia sulcata toxin II reveal conformational heterogeneity in both molecules. The two conformations, manifest in a number of split ¹H resonances, are in slow exchange over a wide range of pH and temperature. Heterogeneity affects a region of these molecules containing the structurally and functionally important Asp residues. By comparison with a homologous polypeptide Anemonia sulcata toxin I, which does not show this type of heterogeneity, it is suggested that the heterogeneity may originate in cis-trans isomerism of the Gly-40 to Pro-41 peptide bond.

Original language	English
Pages (from-to)	15-19
Number of pages	5
Journal	FEBS Letters
Volume	174
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(84)81068-6
Publication status	Published - 20 Aug 1984
Externally published	Yes

Keywords

H-NMR
Cardiotonic agent
Neurotoxin
Peptide conformation
pH titration
Proline

Access to Document

10.1016/0014-5793(84)81068-6

Link to publication in Scopus

Cite this

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title = "Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones",

abstract = "High-resolution 1H NMR spectra at 300 MHz of the polypeptide cardiac stimulants anthopIeurin-A and Anemonia sulcata toxin II reveal conformational heterogeneity in both molecules. The two conformations, manifest in a number of split 1H resonances, are in slow exchange over a wide range of pH and temperature. Heterogeneity affects a region of these molecules containing the structurally and functionally important Asp residues. By comparison with a homologous polypeptide Anemonia sulcata toxin I, which does not show this type of heterogeneity, it is suggested that the heterogeneity may originate in cis-trans isomerism of the Gly-40 to Pro-41 peptide bond.",

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AU - Gooley, Paul R.

AU - Blunt, John W.

AU - Norton, Raymond S.

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N2 - High-resolution 1H NMR spectra at 300 MHz of the polypeptide cardiac stimulants anthopIeurin-A and Anemonia sulcata toxin II reveal conformational heterogeneity in both molecules. The two conformations, manifest in a number of split 1H resonances, are in slow exchange over a wide range of pH and temperature. Heterogeneity affects a region of these molecules containing the structurally and functionally important Asp residues. By comparison with a homologous polypeptide Anemonia sulcata toxin I, which does not show this type of heterogeneity, it is suggested that the heterogeneity may originate in cis-trans isomerism of the Gly-40 to Pro-41 peptide bond.

AB - High-resolution 1H NMR spectra at 300 MHz of the polypeptide cardiac stimulants anthopIeurin-A and Anemonia sulcata toxin II reveal conformational heterogeneity in both molecules. The two conformations, manifest in a number of split 1H resonances, are in slow exchange over a wide range of pH and temperature. Heterogeneity affects a region of these molecules containing the structurally and functionally important Asp residues. By comparison with a homologous polypeptide Anemonia sulcata toxin I, which does not show this type of heterogeneity, it is suggested that the heterogeneity may originate in cis-trans isomerism of the Gly-40 to Pro-41 peptide bond.

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KW - Neurotoxin

KW - Peptide conformation

KW - pH titration

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