Installation of a rigid EDTA-like motif into a protein α-helix for paramagnetic NMR spectroscopy with cobalt(II) ions

James D Swarbrick, Phuc Ung, Matthew L Dennis, Michael D Lee, Sandeep Chhabra, Bim Graham

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix leads to generation of an EDTA-like metal ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies. Do not bend: Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix (see figure) leads to generation of an EDTA-like metal-ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies.

Original languageEnglish
Pages (from-to)1228-1232
Number of pages5
JournalChemistry - A European Journal
Volume22
Issue number4
DOIs
Publication statusPublished - 22 Jan 2016

Keywords

  • alpha-helix
  • cobalt
  • paramagnetic NMR spectroscopy
  • protein structures
  • pseudo-contact shifts

Cite this

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title = "Installation of a rigid EDTA-like motif into a protein α-helix for paramagnetic NMR spectroscopy with cobalt(II) ions",
abstract = "Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix leads to generation of an EDTA-like metal ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies. Do not bend: Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix (see figure) leads to generation of an EDTA-like metal-ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies.",
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Installation of a rigid EDTA-like motif into a protein α-helix for paramagnetic NMR spectroscopy with cobalt(II) ions. / Swarbrick, James D; Ung, Phuc; Dennis, Matthew L; Lee, Michael D; Chhabra, Sandeep; Graham, Bim.

In: Chemistry - A European Journal, Vol. 22, No. 4, 22.01.2016, p. 1228-1232.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Ung, Phuc

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AU - Lee, Michael D

AU - Chhabra, Sandeep

AU - Graham, Bim

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AB - Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix leads to generation of an EDTA-like metal ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies. Do not bend: Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i+4 arrangement within a protein α-helix (see figure) leads to generation of an EDTA-like metal-ion-binding motif. Rigid binding of a CoII ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies.

KW - alpha-helix

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