Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE)

Michaël L Deschamps, Ewa S Pilka, Jennifer R Potts, Iain D Campbell, Jonathan Boyd

Research output: Contribution to journalArticlepeer-review


Nitroxide species, which have an unpaired electron localized on a nitrogen atom, can be useful as NMR probes to identify areas of the surface of a protein involved in the formation of a complex. The proximity of an electron spin leads to higher NMR relaxation rates for protein nuclei. If a protein-ligand complex is formed the radical is excluded from certain sites on the protein surface, protecting them from relaxation effects. We show here that charged nitroxide species can be helpful for identifying regions of the surface of the 4F1(5)F1 module pair from human fibronectin involved in peptide binding.
Original languageEnglish
Pages (from-to)155-60
Number of pages6
Issue number2
Publication statusPublished - 2005


  • Binding Sites
  • Free Radicals
  • Humans
  • Models, Molecular
  • Nitrogen
  • Nitrogen Oxides
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides
  • Protein Binding
  • Protein Structure, Tertiary
  • Proteins
  • Protons
  • Static Electricity

Cite this