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

Cite this

Gooley, P. R., Blunt, J. W., & Norton, R. S. (1984). Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones. FEBS Letters, 174(1), 15-19. https://doi.org/10.1016/0014-5793(84)81068-6

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10.1016/0014-5793(84)81068-6

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