Unknown

Dataset Information

0

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

altmetric image

Publications

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]

Similar Datasets

| S-EPMC2768475 | biostudies-literature
| S-EPMC1220316 | biostudies-other
| S-EPMC2224176 | biostudies-literature
| S-EPMC3397145 | biostudies-literature
| S-EPMC8558257 | biostudies-literature
| S-EPMC3216499 | biostudies-literature
| S-EPMC3582877 | biostudies-literature
| S-EPMC4923719 | biostudies-literature
| S-EPMC6087878 | biostudies-literature