title: Biophysical investigations of the prion protein using electron paramagnetic resonance.
abstract: The binding of paramagnetic metal ions is thought to be an essential function of the prion protein and lends itself to interrogation by electron paramagnetic resonance (EPR), which probes the local coordination environment of bound metal ions to provide details of the metal-binding affinity, stoichiometry, and the symmetry and identity of its ligating atoms. It is also capable of identifying reactive oxygen/nitrogen species and peptide-derived radicals, in addition to monitoring protein-membrane dynamics and conformation by using site-directed spin labeling. An overview of the EPR technique as applied to the prion protein is given, key results are summarized, and some future experimental avenues are outlined.
authors.affiliation: Department of Pathology and Mental Health Research Institute of Victoria, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia.
authors.forename: Simon C
authors.initials: SC
authors.lastname: Drew
authors.forename: Kevin J
authors.initials: KJ
authors.lastname: Barnham
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D018621:PrPC Proteins / Q000032:analysis* / Q000737:chemistry*; D017434:Protein Structure, Tertiary
chemical_list: D002352:Carrier Proteins; D018621:PrPC Proteins; C023548:copper-binding protein