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Copper(II) binding to alpha-synuclein, the Parkinson's protein.


ABSTRACT: Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with alpha-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (Kd 100 nM) near the N-terminus at pH 7. Work on a F4W/H50S mutant indicates that a histidine imidazole is not a ligand in this high-affinity site.

SUBMITTER: Lee JC 

PROVIDER: S-EPMC2664836 | biostudies-other | 2008 Jun

REPOSITORIES: biostudies-other

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Copper(II) binding to alpha-synuclein, the Parkinson's protein.

Lee Jennifer C JC   Gray Harry B HB   Winkler Jay R JR  

Journal of the American Chemical Society 20080509 22


Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with alpha-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (Kd 100 nM) near the N-terminus at pH 7. Work on a F4W/H50S mutant indicates that a histidine imidazole is not a ligand in this high-affinity site. ...[more]

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