Installation of a Rigid EDTA-Like Motif into a Protein α-Helix for Paramagnetic NMR Spectroscopy with Cobalt(II) Ions

Chemistry. 2016 Jan 22;22(4):1228-32. doi: 10.1002/chem.201503139. Epub 2015 Dec 17.

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 Co(II) ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies.

Keywords: alpha-helix; cobalt; paramagnetic NMR spectroscopy; protein structures; pseudo-contact shifts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cobalt / chemistry*
  • Edetic Acid / chemistry*
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Protein Binding

Substances

  • Ligands
  • Cobalt
  • Edetic Acid