Cu2+ binding modes of recombinant α-synuclein - Insights from EPR spectroscopy

Journal of the American Chemical Society

Volumn 130, Issue 24, 2008, Pages 7766-7773

  Drew, Simon C ^a,b,c,d   Su, Ling Leong ^a,b   Pham, Chi L L ^a,b,d   Tew, Deborah J ^a,b,d   Masters, Colin L ^a,d   Miles, Luke A ^e   Cappai, Roberto ^a,b,d   Barnham, Kevin J ^a,b,d  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c MONASH UNIVERSITY   (Australia)

^d FLOREY INSTITUTE OF NEUROSCIENCE AND MENTAL HEALTH   (Australia)

^e TOKYO METROPOLITAN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; HEALTH; ORGANIC ACIDS;

SYNUCLEIN;

COPPER ALLOYS;

ALPHA SYNUCLEIN; ASPARTIC ACID; COPPER; DIETHYL PYROCARBONATE; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ELECTRON SPIN RESONANCE; MOLECULAR INTERACTION; MOLECULAR MODEL; MUTATION; PH; PROTEIN BINDING; STOICHIOMETRY; WILD TYPE; BINDING SITE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS;

ALPHA-SYNUCLEIN; BINDING SITES; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; MUTATION; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS;

EID: 45249097302     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja800708x     Document Type: Article

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44. The latter possibility would imply Figure 1c was comprised of two overlapping spectra, which might explain the absence of shf structure in this instance.