Published June 4, 2008
| Supplemental Material + Published
Journal Article
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Copper(II) Binding to α-Synuclein, the Parkinson's Protein
Chicago
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Abstract
Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with α-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (K_d ∼ 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.
Additional Information
© 2008 American Chemical Society. ACS AuthorChoice. Received December 26, 2007; Publication Date (Web): May 9, 2008. Supported by the Intramural Research Program of the National Institutes of Health, the National Heart, Lung, and Blood Institute (JCL), and grants from the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.) and NIH (GM068461 to J.R.W.; DK19038 to H.B.G.). Initial work was supported by a Beckman Senior Research Fellowship (J.C.L.).Attached Files
Published - ja711415b.pdf
Supplemental Material - ja711415b-file002.pdf
Supplemental Material - ja711415b-file003.pdf
Supplemental Material - ja711415b-file004.pdf
Supplemental Material - ja711415b-file005.pdf
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Additional details
- PMCID
- PMC2664836
- Eprint ID
- 74809
- Resolver ID
- CaltechAUTHORS:20170306-150523974
- Ellison Medical Foundation
- NIH
- GM068461
- NIH
- DK19038
- Arnold and Mabel Beckman Foundation
- Created
-
2017-03-07Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field