Applications of electron paramagnetic resonance to studies of neurological disease.
Electron paramagnetic resonance spectroscopy (EPR) has the potential to give much detail on the structure of the paramagnetic transition ion coordination sites, principally of Cu2+, in a number of proteins associated with central nervous system diseases. Since these sites have been implicated in misfolding/mis-oligomerisation events associated with neurotoxic molecular species and/or the catalysis of damaging redox reactions in neurodegeneration, an understanding of their structure is important to the development of therapeutic agents. Nevertheless EPR, by its nature an in vitro technique, has its limitations in the study of such complex biochemical systems involving self-associating proteins that are sensitive to their chemical environment. These limitations are at the instrumental and theoretical level, which must be understood and the EPR data interpreted in the light of other biophysical and biochemical studies if useful conclusions are to be drawn.
Boas
John F
JF
School of Physics, Monash University, Clayton, VIC 3800, Australia. john.boas@sci.monash.edu.au
Drew
Simon C
SC
Curtain
Cyril C
CC
D016229:Amyloid beta-Peptides / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D004578:Electron Spin Resonance Spectroscopy / Q000639:trends*; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D009422:Nervous System Diseases / Q000503:physiopathology*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D013113:Spin Labels; D014894:Weights and Measures; D051844:alpha-Synuclein / Q000378:metabolism
D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D013113:Spin Labels; D051844:alpha-Synuclein; D003300:Copper