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

27 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

Cite this

@article{1af2ba140e2845b9b0a9182f9c50cce1,

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.",

keywords = "H-NMR, Cardiotonic agent, Neurotoxin, Peptide conformation, pH titration, Proline",

author = "Gooley, {Paul R.} and Blunt, {John W.} and Norton, {Raymond S.}",

year = "1984",

month = aug,

day = "20",

doi = "10.1016/0014-5793(84)81068-6",

language = "English",

volume = "174",

pages = "15--19",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons",

number = "1",

}

TY - JOUR

T1 - Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones

AU - Gooley, Paul R.

AU - Blunt, John W.

AU - Norton, Raymond S.

PY - 1984/8/20

Y1 - 1984/8/20

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.

KW - H-NMR

KW - Cardiotonic agent

KW - Neurotoxin

KW - Peptide conformation

KW - pH titration

KW - Proline

UR - http://www.scopus.com/inward/record.url?scp=0021767567&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(84)81068-6

DO - 10.1016/0014-5793(84)81068-6

M3 - Article

C2 - 6147271

AN - SCOPUS:0021767567

VL - 174

SP - 15

EP - 19

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -

Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones

Abstract

Keywords

Access to Document

Other files and links

Cite this